NCBI Bookshelf. A service of the National Library of Medicine, National Institutes of Health.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.

Cover of Madame Curie Bioscience Database

Madame Curie Bioscience Database [Internet].

Show details

Diversity of WD-repeat Proteins


Temple F. Smith—BioMolecular Engineering Research Center, College of Engineering, Boston University, 36 Cummington Street, Boston, MA 02215, USA. Email: ude.ub.niwrad@htimst

The Coronin Family of Proteins, edited by Christoph S. Clemen, Ludwig Eichinger and Vasily Rybakin.
Read this chapter in the Madame Curie Bioscience Database here.

The WD-repeat-containing proteins form a very large family that is diverse in both its function and domain structure. Within all these proteins the WD-repeat domains are thought to have two common features: the domain folds into a beta propeller; and the domains form a platform without any catalytic activity on which multiple protein complexes assemble reversibly. The fact that these proteins play such key roles in the formation of protein-protein complexes in nearly all the major pathways and organelles unique to eukaryotic cells has two important implications. It supports both their ancient and proto eukaryotic origins and supports a likely association with many genetic diseases.


Many protein families are characterized by their common sequence motifs, catalytic function and/or structure. WD-repeat domain-containing proteins comprise one such family characterized by a common sequence repeat named for the high frequency of the tryptophan and aspartic acid pairs that generally define the end of its approximately 40-residue-long amino acids. While the sequence repeat contains no absolutely conserved positions, the basic pattern is well-conserved (see Fig. 1A). Structurally the domains containing these repeats belong to the larger class of proteins having the beta propeller fold. These are highly symmetric folds composed of between four and eight anti-parallel, four-stranded beta sheets arranged radially around a central axis, as shown in Figure 1B. In the case of the WD-repeat-containing proteins, each WD repeat is part of one of the four anti-parallel strands that form one of the “blades” of these propeller-like structures. The full WD sequence-repeat is not equivalent to a single blade, but rather each contains the first three strands of one blade and the fourth of the adjacent blade. While beta propeller structures are found throughout both Prokaryota and Eukaryota, the WD-repeat beta propellers are found primarily among eukaryotes.1

Figure 1. The beta WD propeller.

Figure 1

The beta WD propeller. A) The repeat-defining sequence's most common amino acids. “x” indicates any amino acid. Number in brackets indicate the known variable range. B) The F-box WD-repeat protein 1p22.pdb (beta-TrCP1) with dark gray strand (more...)

There is no common function within the larger protein structural family of the beta propellers, as is true for most families defined only by their common fold. At one level this is also true within the WD sequence repeat family, where there is no common function in terms of substrate binding, catalytic activity or pathway membership. What does appear to be the common feature is the ability of that domain to interact reversibly with multiple other proteins to form complexes.2 It forms a stable platform or scaffold on which large protein-protein complexes assemble. This WD-repeat-containing domain is found throughout Eukaryota, ranging from a few to over a hundred distinct proteins in mammals. It functions in signal transduction, RNA processing, vesicular trafficking, cytoskeleton assembly, cell cycle regulation, transcription of the initiation complex and many other processes (see Table 1).

Table 1. A partial list of cellular pathways and functions involving WD-repeat-containing proteins.

Table 1

A partial list of cellular pathways and functions involving WD-repeat-containing proteins.

Figure 1B,C displays a typical WD-repeat protein, beta-TrCP1 ubiquitin ligase. This protein is a multidomain protein containing both a WD and an F-box domain (mediates interaction withSkp1 linking F-box proteins to a ubiquitin-ligase complex). It, like many WD-repeat proteins, contains both an insert within the WD-repeat domain forming an additional small structure on one of the domain's surfaces and is multidomained. The F-box WD-repeat combination proteins form a rather large family. This includes Pop1 and Pop2 proteins, which in yeast play a key role in cell cycle progression.3

Perhaps the best studied member of this family is the beta subunit of the trimeric G-protein, a key signal transduction system found throughout Eukaryota.4 In this case, nearly the entire beta subunit consists of seven WD sequence repeats that form a seven-bladed beta propeller.5-7 In addition there is a short alpha helical domain at the C-terminal end that binds nearly irreversibly to the gamma subunit (composed of only two alpha helices). One additional curious fact is that at least in the case of Dictyostelium, this G-beta-gamma combination requires an additional protein, PhLP18 for assembly. This beta-gamma G-protein subunit interacts with the catalytic alpha subunit in its inactive receptor bound state. The activation of the G-protein receptor catalyzes the exchange of GDP in the alpha subunit for GTP. Tat in turn causes the separate release from the receptor of the G-beta-gamma subunit and the G-alpha subunit. Both then interact reversibly with a number of other downstream proteins within various signaling cascades.9-12

The Beta Propeller Structure

This common fold variously contains from four to nine anti-parallel four-stranded beta sheets.1 These are arrayed radially with a geometry similar to a ship's propeller, each propeller blade being composed of four anti-parallel strands, each slightly twisted in the same orientation. The height or length of the strands within each blade is near constant within a given protein, but can vary over a rather wide range from a minimum of four to 10 amino acids in different proteins. These structures define three surfaces, a circular top and bottom and a cylindrical circumference. In many cases part of the cylindrical surface is in contact with one or more additional domains that are part of the same protein. For example, in the above noted trimeric G-protein beta subunit, there is the short helical domain contacting part of both the cylindrical and the bottom surfaces. In the archaeal surface layer beta propeller protein, SLP,13 there are multiple copies of a second all-beta domain making extensive surface contacts with the beta propeller domain. The latter protein is a particularly interesting example. It, like the G-protein WD beta subunit, forms a seven-bladed propeller and contains a sequence repeat with a distinctive YVTN amino acid motif. This protein in fact contains two very similar seven-bladed beta propellers and 12 repeated small all-beta domains (see Fig. 3 in Jing et al 2002).13 In addition, it shows similarity to a metazoan cell surface set of seven-bladed beta propeller protein receptors that contain the YWTD motif.13 The similarity in both cellular location and sequence motif suggests a potential common origin of these proteins. As discussed below, however, there is no such similar example to guide us in attempting to identify the ancestor of the eukaryotic WD-repeat proteins. Kostlanova et al14 identified a beta propeller from Ralstonia solanacearum formed by oligomerization rather than being contained within a single peptide as are other known beta propeller proteins, including all known WD-repeat domains.

There are other beta propeller families with very similar fold structures to the WD-repeat family, such as the EAR domain family. These form seven-bladed propellers with amino acid repeats averaging 44 residues long.15 Interestingly they have a weakly conserved sequence motif that includes a tryptophan polar amino acid pair at the end of the fourth strand, as compared to the tryptophan aspartic acid pair common to the end of the third strand in the WD-repeat family. Also like the WD-repeat domain, the EAR domain generally occurs within a larger multidomain protein. One structural fact about the WD-repeat beta propellers and other beta propeller families is that the amino acid composition internal to the region of beta sheet-to-sheet contacts does not vary as a function of the number of repeats. Thus as the overall size increases, from four to more blades, any needed change in the side chain packing is compensated by slight changes in blade twist and side chain rotomers. This again seems to support the idea of a very stable fold configuration for these proteins. However as seen in Figure 1B, the WD-repeat proteins close their propeller circular structures with a Velcro-like overlap of the third strand of the last blade with an outer strand from the first of the WD repeats. Many nonWD propellers do not use this closure method. For example the YWTD motif-containing propellers form all blades sequentially, each containing the complete sequence repeat.

The Identification of WD Repeats

Given the variation in size, composition, function and domain structure the accurate identification of all WD-repeat-containing proteins has been a challenge. As an example, the distribution of WD-repeat-containing proteins in plants has been investigated in the model system, Arabidopsis, by van Nocker and Ludwig.16,17 They identified 237 potential WD-repeat-containing proteins falling into what they believed to be more than 50 distinct families. Their approach involved identifying all Arabidopsis proteins containing at least four WD-repeat patterns as defined by patterns and/or examples in Prosite, Pfam, PRINTS and SMART.18 These were then clustered using Blastclust ( This is a rather straightforward general approach, similar to that employed by the BioMolecular Engineering Research Center at Boston University, which maintains the WD-repeat database (on the web at The basic sequence repeat can be identified as a weakly conserved motif, as shown in Figure 1A, with an overall sequence compatibility with a probable structure.

The difficulty in identifying members of WD-repeat families is two-fold: first the pattern is not absolutely conserved, even in part; and second, in any standard sequence comparison search, the different repeats in a given protein will match many WD repeats in a wide range of different family representatives over a very wide range of statistical significance. The variation in the number of blades within different subfamilies of WD-repeat proteins and the fact that different WD-repeat families often contain at least one of the same additional domains, makes subfamily distinction difficult. This difficulty can be acute and is compounded by the fact that WD-repeat proteins often have one or more such nonWD domains inserted within and between the WD repeats that form a single beta propeller (see Fig. 1B,C).

The seven-bladed propeller structure of the coronin family contains only five clearly identifiable WD repeats. These WD repeats are found between positions 79 and 305 in the murine coronin 1 (coronin 1A).19 The first and last blades, 37-71 and 306-352 are either very highly modified WD repeats or were derived from a different source. While it is possible that five WD repeats were inserted into some pre-existing beta domain, this seems a bit unlikely given the standard Velcro-type propeller closure is employed. In addition the strand order in these two non WD repeats is the same as that in the five WD repeats. It is clear that the sequences of these two non WD repeats are by themselves diagnostic of the coronin family.

There is a curious and characteristic feature of the WD-repeat domains. This is that the most conserved position for a particular amino acid in the WD repeat is not in the “defning” trp/asp pair at the end of the third strand, but an aspartic acid in the turn between the second and third strand of each propeller blade. This amino acid position effectively forms a highly polar, normally negative charged ring on the top of the propeller. A second feature containing a very limited range of amino acids (see Fig. 1A) is the run of three small side chain amino acids at the C-terminal end of the second blade's strand. Finally there is the turn/loop region between strands 1 and 2, which while often varying in length, generally contains a proline aspartic acid or aspartate glycine classic reverse turn. Such distinctive features often allow the identification of the WD repeat even when other features are either missing or weak.

The above considerations require an iterative approach in which one first identifies all highly probable WD repeats within each protein of interest. Next one attempts to examine the rest of the protein for more divergent repeats that have the expected length and fall in the neighborhood or between clear WD repeats. In addition the sequence must be examined for other domains that may interrupt the sequence of WD repeats, but are known to occur in some WD families. Finally there must be a reasonable probability that there are at least four WD repeats, as no beta propeller is stable with fewer than four blades. There is also the likelihood that this structure is limited to no more than nine blades, as the central axis would be open to the solvent, reducing its stability. Under the assumption that it is the WD-repeat domain's surfaces that primarily define its role in protein-protein interactions, common features among the surface amino acids should be useful in identifying members of any given WD-repeat subfamily.

There are numerous sequence pattern tools to carry out the initial step above. There is, however, no single obvious approach for the remaining steps. One useful approach is the use of a set of probabilistic Hidden Markov Models.20 Such models allow one to assign probabilities or likelihoods to the WD-repeat pattern elements individually, to the total number of such repeats, to their length ranges and to the chance and lengths of likely inserted non WD-repeat domains (see schematic in Fig. 1B,C). The probabilities used in such an HMM are determined either by observational experience using protein expert knowledge to anticipate yet unseen variations,20 or by computational model training algorithms21 on sets of known examples. In any case while a very large number of WD-repeat proteins can be straightforwardly recognized, there are undoubtedly both false positives and missed examples in both the literature and the annotated databases. Thus there is some uncertainty within the representative species distribution statistics given in Table 2.

Table 2. Distribution of WD-repeat counts in WD proteins among a set of representative eukaryotic species. The number pairs are the total probable WD proteins with a given range of repeats. In parentheses is the subset of those that contain at least one significant additional non WD domain.

Table 2

Distribution of WD-repeat counts in WD proteins among a set of representative eukaryotic species. The number pairs are the total probable WD proteins with a given range of repeats. In parentheses is the subset of those that contain at least one significant (more...)

While the WD-repeat proteins are rare in Prokaryota, there have been five identified among the 500-plus sequenced bacterial genomes, for example, the noncanonical WD-repeats of Hat found in the cyanobacterium Synechocystis.22 This protein is involved in inorganic carbon transport and has five significant repeats matching the pattern shown in Figure 1A. It also has five or six additional weaker repeats with the potential for a total of eleven.

The Functions Carried Out by the WD-repeat Family

These proteins are involved in a very wide range of cellular functions. In all cases studied in detail, the actual beta propeller WD-repeat domain is not involved in any catalytic function. This is in contrast to many beta propeller, nonWD-repeat domains, as in the case of the fructosyl transferases.23 As noted above, the WD-repeat domains provide multiple protein-protein binding surfaces for reversible protein complex formation.2 A particularly interesting example has been seen in the East African cichlid fishes, the hag gene.24 This is a member of the large class of the F-Box joint WD-repeat family known to regulate differentiation in the fly25 What was observed in the cichlid fish was a very rapid speciation correlated with accelerated surface amino acid selected changes on the WD-repeat domain. This clearly suggests that some of the speciation defining genetic events could be seen in the selective adaptation within these interacting surfaces effecting changes in pigment pattern.24 The WD-repeat-containing protein, Wdr526 also plays a key role in differentiation, in this case that of osteoblasts and chondrocytes. There are a number of other well-studied examples of these surface protein-protein interactions11,12 directly observed for various WD-repeat-containing proteins. These include the TFDII, required for transcription initiation complex formation and the IC138 and IC140 WD-repeat proteins required for dynein inner-arm motor complex formation in eukaryotic cilia.27 A third WD-repeat protein, IFTA-1, is also involved in cilia assembly, in this case for the retrograde intraflagellar protein transport.28 Identified in Dictyostelium is another WD protein, MHCK, which is involved with another motor protein, myosin. Here the WD-domain targets the myosin heavy chain kinases by binding to the myosin filaments.29 One very well-studied WD-repeat protein is Lis1, a protein that regulates the microtubule motor cytoplasmic dynein, while in the vertebrate brain it is associated with the cytosolic PAF-acetylhydrolase. This interaction has been studied in a high resolution crystal structure revealing major protein-protein contacts with the upper circular surface of the WD domain.30

There is a WD yeast protein, Swd2, that plays an essential role in two distinct complex assemblies, the assembly of the peptide cleavage and polyadenylation factor and that of the lysine methylation of histone H3 complex.31 More typical is the yeast protein, Mdv1p, that plays a key role in the assembly of a single complex, the mitochondrial division, Dnm1p, complex in conjunction with the mitochondrial outer membrane protein Fis1P.32 In Arabidopsis the SPA1 protein is involved in phytochrome A-signal transduction complex33 and is an example of a WD-repeat domain attached to a catalytic domain, in this case a kinase domain. There is a pair of WD-repeat proteins, Mad2 and BubR1, that together yield the kinetochore complex, involved in interaction with a histone deacetylase.34 The complex appears capable of delaying anaphase by inhibiting ubiquitin ligation.

The Gemin5 WD-repeat protein interacts with at least five of the snRNP core proteins in forming the SMN complex.35 This is a large protein with 13 predicted WD repeats and a C-terminal coiled-coil domain. The coiled-coil domain, like the WD itself, is a protein-protein interaction domain. The large number of WD repeats in Gemin5 suggests that there are probably two WD domains, one of seven repeats and a second of six or seven repeats. The probability of three protein-protein interaction domains creates the possibility of forming a very large heteromeric complex or of being capable of forming multiple but distinct ones. There are other WD-repeat proteins that contain additional protein-protein interaction domains. Tree of these are found in the brain and are members of the striatin family containing a coiled-coil domain and calmodulin-binding domain36 in addition to a WD domain. Two of these are expressed in the central nervous system and are somehow involved in dendrite growth while another, SG2NA, is expressed in both brain and muscle. All three are both cytosolic and membrane-bound.36 Another WD-repeat protein, NDRP, is associated with neurons and is expressed in developing and regenerating neurons, particularly those of the olfactory epithelia and retina.37

The GRWD1, a large protein containing a glutamate-rich domain and four WD-repeats, with a second WD-repeat protein, Bop1, is part of the preribosomal complex in ribosomal biogenesis.38 A WD-repeat protein with a related function is the Ras4p, which along with being required for 60S ribosomal transport is required for tRNA processing. As a final example, the SIF2 WD-repeat yeast protein containing an eight-bladed WD propeller39 is key to the assembly of the Set3 complex. This complex is the histone deacetylase complex and a meiosis-specific repressor of sporulation genes. It is worthy of note that the top surface of this protein is highly conserved. A second domain in the SIF2 protein mediates its tetramerization and its eight-bladed propeller structure is distinct as a corepressor as compared to other corepressor families such as the Groucho WD-repeat family.40 This WD protein plays an extensive role in gene expression associated with developmental patterning.41 While the Groucho proteins do not bind DNA directly they appear to bind other proteins that do. The role of WD-repeat proteins in both animal and plant embryo patterning and development is well documented. For example the Xbub3 protein is distributed throughout the oocyte in the early stages and then gradually localized to the animal hemisphere in the perinuclear cytoplasm of mature oocytes.42 While in the plant Arabidopsis the WD-repeat protein, TAN, has been shown to be required of embryo development via its interactions with other proteins.43

In a short review of the Human WD-repeat proteins Li and Roberts44 noted their association with a number of human diseases. Some WD-repeat family proteins have been directly implicated in a particular human disease. For example the G-protein beta-3 subunit appears to have a splice variant that is causal in essential hypertension.45 The Triple-A syndrome has been shown to be caused by mutations in the WD-repeat protein, AAAS.46 The WD-repeat protein WAIT-1 is known to interact with the beta-7 integrins and affects lymphocyte homing in the normal immune response47 and its mutation can disrupt that part of the immune response. The WD-repeat protein STRAP has an oncogenic affect in human carcinogenesis apparently through its interaction with transforming growth factor, TGF-beta.48 The WD-repeat protein, endonulein, as a cell cycle protein is an oncogene for adenocarcinoma of the pancreas when up-regulated.49 The human WDR11 protein is associated with glioblastoma via a chromosome translocation truncating the WD-repeat domain after the second of six repeats.50 The Groucho family, which is key in developmental patterning as an organizer of gene repression, may play a role in colorectal cancer suppression via the Wnt signaling pathway.51 There is a set of mutations in the WD-repeat domain of AHI1 that is associated with the autosomal recessive disorder, Houbert syndrome, involving mental retardation.52 While this is only a short list of examples of WD domain disease correlations, the current functional list (in Table 1) of WD-repeat domain-containing protein functions is suggestive of a much wider range of potential inherited-disease associations.

There are of course many other functional complexes containing or organized by WD-repeat domains. Many of these involve signal transduction, the best studied being the large number of known trimeric G-proteins and their downstream complexes generally involving MAP Kinase cascades. Table 1 contains a list of these and other cellular functions, roles and/or pathways in which at least one WD-repeat-containing protein has been clearly shown. Included of course are the members of the actin binding family of coronin proteins discussed throughout the following chapters.

The Distribution and Origin of the Family

Table 2 lists the number of WD-repeat protein sequences identified with high confidence within various taxonomic divisions for particular species representatives. The numbers were obtained using simple sequence pattern recognition tools followed by a full-length protein sequence context analysis. They are presented in terms of the number of probable WD repeats and whether or not they contain additional domains of significant length.

The limited occurrences of WD repeats in the prokaryotic taxa raise the issue as to whether this family is of very ancient origin or, as has been suggested, is a eukaryotic invention borrowed by some prokaryotes via horizontal gene transfer. Given the very wide range in sequence, blade number and functions found among the beta propellers, one might wonder if they all had a common early ancestor. Or is it more likely that this fold is so naturally stable that nearly any four-fold plus repeat with high beta propensity of 36 to 50 amino acids will form this type of structure? Repeats at the DNA level are common mutational fare in all organisms. The possible eukaryotic origin is supported by the fact that so many of the WD-repeat proteins are involved in forms of signal transduction pathways unique to the eukaryotes. In addition few of the prokaryotic WD-repeat domain-containing protein examples have clear homologs in other prokaryotes. Also given the domain's ability to form large complexes, it could easily find utility if taken up by a prokaryote. Yet the potential homology of the archaeal surface layer protein (SLP)13 YVTN-repeat seven-bladed beta propeller and the metazoan cell surface YWTD-repeat seven-bladed beta propeller cell surface receptors13 supports a common ancestral relationship between these prokaryotic and eukaryotic protein families.

Most attempts at standard sequence phylogenetic analyses are difficult and/or inconclusive due to the high similarity within the structure-determining features of the WD repeats, overwhelming the functional family surface characteristics. By masking the beta propeller's internal repeat residues and then clustering only on the basis of the remaining sequence, there has been some success in functional grouping of the WD-repeat proteins. For example, surface analysis of one pair of proteins, MSI1 and Rb48 clustered them in the same subfamily, while the entire WD-repeat domain did not.2 This clustering was verified by their partial complementation in yeast. Yet this did not allow any clear evolutionary relationships to emerge among these clustered functional subfamilies. Given that repeats are common in most beta propeller families of between four and eight blades, gene region expansion by duplication and contraction by deletion appears to have occurred many times. The fact that there are so many distinct repeat encoding beta propellers supports such a simple common genetic mechanistic origin. Yet given that these structures require at least four blades, one must also assume that some of these distinct families could have arisen through oligomerization as homo-tetramers or -dimers, as seen in Ralstonia solanacearum.14

Once a repeat is discovered to form a stable protein propeller platform, the sequence repeats can apparently be maintained and recognizable over a very long evolutionary period. There clearly has been functional selection on the surface residues and as to what additional domains are linked. On the other hand, negative or conserving selection appears to have been restricted to internal blade-to-blade packing, at least among this very large and diverse WD-repeat family. Given this variation in conserved repeats within, but not between, families, most repetitive beta propeller families seem likely to have independent origins. As for the origin of the WD-repeat superfamily, little is known. Without considerably more detailed information on the functions of the limited number of WD-repeat proteins found in prokaryotes one can only guess that the WD-repeat family is likely of eukaryotic origin. Tat of course would require that their occurrence in Prokaryota was probably the result of one or more horizontal gene transfer events. The issue is one of their distributional ubiquity in all Eukaryota, including components of so many unique eukaryotic functions, compared to limited and noncommon functions among the prokaryotes. While the eukaryotic WD-repeat families do seem to have the common function of protein-protein binding and complex assemblies, which if any of these was the first is very unclear. Signal transduction via the trimeric G-proteins of course is a possibility, but so is the essential role in RNA processing, in cilia or cytoskeleton assembly and in the initiation of transcription, all of which have been suggested as components of the last common ancestor of all extant eukaryotes. What is clear is that once this protein complex assembly aid was discovered, it was rapidly exploited throughout the earliest eukaryotes.


Paoli M. Protein folds propelled by diversity. Prog Biophys Mol Biol. 2001;76(1-2):103–30. [PubMed: 11389935]
Smith TF, Gaitatzes C, Saxena K. et al. The WD repeat: a common architecture for diverse functions. Trends Biochem Sci. 1999;24(5):181–85. [PubMed: 10322433]
Kominami K, Ochotorena I, Toda T. Two F-box WD-repeat proteins Pop1 and Pop2 form hetero- and homo-complexes together with cullin-1 in the fission yeast SCF (Skp1-Cullin-1-F-box) ubiquitin ligase. Genes Cells. 1998;3:721–35. [PubMed: 9990507]
Neer EJ. Heterotrimeric G-Proteins—Organizers of Transmembrane Signals. Cell. 1995;80(2):249–57. [PubMed: 7834744]
Lambright DG, Sondek J, Bohm A. et al. The 2.0 angstrom crystal structure of a heterotrimeric G protein. Nature. 1996;379(6563):311–19. [PubMed: 8552184]
Neer EJ, Smith TF. G protein heterodimers: New structures propel new questions. Cell. 1996;84(2):175–78. [PubMed: 8565060]
Wall MA, Coleman DE, Lee E. et al. The Structure of the G-Protein Heterotrimer G(I-Alpha-1) Beta(1)Gamma(2) Cell. 1995;83(6):1047–58. [PubMed: 8521505]
Knol JC, Engel R, Blaauw M. et al. The Phosducin-Like Protein PhLP1 Is Essential for Gß Dimer Formation in Dictyostelium discoideum. Mol Cell Biol. 2005;25(18):8393–400. [PMC free article: PMC1234308] [PubMed: 16135826]
Cabrera-Vera TM, Vanhauwe J, Thomas TO. et al. Insights into G protein structure, function and regulation. Endocr Rev. 2003;24(6):765–81. [PubMed: 14671004]
Katanaev VL, Tomlinson A. Dual roles for the trimeric G protein Go in asymmetric cell division in Drosophila. Proc Natl Acad Sci USA. 2006;103(17):6524–29. [PMC free article: PMC1436022] [PubMed: 16617104]
Li Y, Sternweis PM, Charnecki S. et al. Sites for G binding on the G protein subunit overlap with sites for regulation of Phospholipase C and Adenylyl. Cyclase J Biol Chem. 1998;273:16265–72. [PubMed: 9632686]
Panchenko MP, Saxena K, Li Y. et al. Sites important for PLC beta(2) activation by the G protein beta gamma subunit map to the sides of the beta propeller structure. J Biol Chem. 1998;273(43):28298–304. [PubMed: 9774453]
Jing H, Takagi J, Liu JH. et al. Archaeal surface layer proteins contain beta propeller, PKD and beta helix domains and are related to metazoan cell surface proteins. Structure. 2002;10(10):1453–64. [PubMed: 12377130]
Kostlanova N, Mitchell EP, Lortat-Jacob H. et al. The fucose-binding lectin from Ralstonia Solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan. J Biol Chem. 2005;280(30):27839–27849. [PubMed: 15923179]
Scheel H, Tomiuk S, Hofmann K. A common protein interaction domain links two recently identified epilepsy genes. Hum Mol Genet. 2002;11(15):1757–62. [PubMed: 12095917]
van Nocker S, Ludwig P. The WD-repeat protein superfamily in Arabidopsis: conservation and divergence in structure and function. BMC Genomics. 2003;4:50. [PMC free article: PMC317288] [PubMed: 14672542]
Zhong R, Ye Z-H. Molecular and Biochemical Characterization of Three WD-Repeat-Domain-containing Inositol Polyphosphate 5-Phosphatases in Arabidopsis thaliana. Plant Cell Physiol. 2004;45(11):1720–28. [PubMed: 15574849]
Mulder NJ, Apweiler R, Attwood TK. et al. The InterPro Database, 2003 brings increased coverage and new features. Nucleic Acids Res. 2003;31(1):315–18. [PMC free article: PMC165493] [PubMed: 12520011]
Appleton BA, Wu P, Wiesmann C. The crystal structure of murine coronin-1. Structure. 2006;14:87–89. [PubMed: 16407068]
Yu L, Gaitatzes C, Neer EJ. et al. Thirty-plus functional families from a single motif. Protein Sci. 2000;9:2470–76. [PMC free article: PMC2144505] [PubMed: 11206068]
Hisbergues M, Gaitatzes CG, Joset F. et al. A noncanonical WD-repeat protein from the cyanobacterium Synechocystis PCC6803: Structural and functional study. Protein Sci. 2001;10(2):293–300. [PMC free article: PMC2373943] [PubMed: 11266615]
Rabiner LR. A Tutorial on Hidden Markov-Models and Selected Applications in Speech Recognition. Proc IEEE. 1989;77(2):257–86.
Pons T, Hernandez L, Batista FR. et al. Prediction of a common beta-propeller catalytic domain for fructosyltranferases of different origin and substrate specificity. Protein Sci. 2000;9:2285–91. [PMC free article: PMC2144480] [PubMed: 11305239]
Terai Y, Morikawa N, Kawakami K. et al. Accelerated evolution of the surface amino acids in the WD-repeat domain encoded by the hagoromo gene in an explosively speciated lineage of east African cichlid fishes. Mol Biol Evol. 2002;19(4):574–78. [PubMed: 11919300]
Jiang J, Struhl G. Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40- repeat protein Slimb. Nature. 1998;391:493–96. [PubMed: 9461217]
Gori F, Friedman L, Demay M. Wdr5, a novel WD repeat protein, regulates osteoblast and chondrocyte differentiation in vivo. J Musculoskelet Neuronal Interact. 2005;5(4):338–39. [PubMed: 16340128]
Hendrickson TW, Perrone CA, Griffin P. et al. IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending. Mol Biol Cell. 2004;15(12):5431–42. [PMC free article: PMC532023] [PubMed: 15469982]
Blacque OE, Li C, Inglis PN. et al. The WD Repeat-containing Protein IFTA-1 Is Required for Retrograde Intraflagellar Transport. MBC. 2006;17(12):5053–62. [PMC free article: PMC1679672] [PubMed: 17021254]
Steimle PA, Naismith T, Licate L. et al. WD repeat domains target Dictyostelium myosin heavy chain kinases by binding directly to myosin filaments. J Biol Chem. 2001;276(9):6853–60. [PubMed: 11106661]
Tarricone C, Perrina F, Monzani S. et al. Coupling PAF signaling to dynein regulation structure of LIS1 in complex with PAF-Acetylhydrolase. Neuron. 2004;44(5):809–21. [PubMed: 15572112]
Cheng HL, He XY, Moore C. The essential WD repeat protein Swd2 has dual functions in RNA polymerase II transcription termination and lysine 4 methylation of histone H3. Mol Cell Biol. 2004;24(7):2932–43. [PMC free article: PMC371121] [PubMed: 15024081]
Tieu Q, Okreglak V, Naylor K. et al. The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission. J Cell Biol. 2002;158(3):445–52. [PMC free article: PMC2173813] [PubMed: 12163467]
Hoecker U, Tepperman JM, Quail PH. SPA1, a WD-repeat protein specific to phytochrome A signal transduction. Science. 1999;284(5413):496–99. [PubMed: 10205059]
Yoon Y, Baek K, Jeong S. et al. WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase. FEBS Lett. 2004;575(1-3):23–29. [PubMed: 15388328]
Gubitz AK, Mourelatos Z, Abel L. et al. Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins. J Biol Chem. 2002;277(7):5631–36. [PubMed: 11714716]
Castets F, Rakitina T, Gaillard S. et al. Zinedin, SG2NA and striatin are calmodulin-binding, WD repeat proteins principally expressed in the brain. J Biol Chem. 2000;275(26):19970–77. [PubMed: 10748158]
Kato H, Chen S, Kiyama H. et al. Identification of a novel WD repeat—containing gene predominantly expressed in developing and regenerating neuron. J Biochem. 2000;128:923–32. [PubMed: 11098134]
Gratenstein K, Heggestad AD, Fortun J. et al. The WD-repeat protein GRWD1: Potential roles in myeloid differentiation and ribosome biogenesis. Genomics. 2005;85(6):762–73. [PubMed: 15885502]
Cerna D, Wilson DK. The structure of sif2p, a WD repeat protein functioning in the SET3 corepressor complex. J Mol Biol. 2005;351(4):923–35. [PubMed: 16051270]
Chen GQ, Courey AJ. Groucho/TLE family proteins and transcriptional repression. Gene. 2000;249(1-2):1–16. [PubMed: 10831834]
Song HY, Hasson P, Paroush Z. et al. Groucho oligomerization is required for repression in vivo. Mol Cell Biol. 2004;24(10):4341–50. [PMC free article: PMC400465] [PubMed: 15121853]
Goto T, Kinoshita T. Maternal transcripts of mitotic checkpoint gene, Xbub3, are accumulated in the animal blastomeres of Xenopus early embryo. DNA Cell Biol. 1999;18(3):227–34. [PubMed: 10098604]
Yamagishi K, Nagata N, Yee KM. et al. TANMEI/EMB2757 encodes a WD repeat protein required for embryo development in Arabidopsis. Plant Physiol. 2005;139(1):163–73. [PMC free article: PMC1203366] [PubMed: 16113228]
Li D, Roberts R. WD-repeat proteins: structure characteristics, biological function and their involvement in human diseases. Cell Mol Life Sci. 2001;58:2085–97. [PubMed: 11814058]
Benjafield AV, Jeyasingam CL, Nyholt DR. et al. G-Protein ß3 subunit gene (GNB3) variant in causation of essential hypertension. Hypertension. 1998;32:1094–97. [PubMed: 9856980]
Handschug K, Sperling S, Yoon SJK. et al. Triple A syndrome is caused by mutations in AAAS, a new WD-repeat protein gene. Hum Mol Genet. 2001;10(3):283–90. [PubMed: 11159947]
Rietzler M, Bittner M, Kolanus W. et al. The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta 7-integrins. J Biol Chem. 1998;273(42):27459–66. [PubMed: 9765275]
Halder T, Pawelec G, Kirkin AF. et al. Isolation of novel HLA-DR restricted potential tumor-associated antigens from the melanoma cell line FM3. Cancer Res. 1997;57(15):3238–44. [PubMed: 9242455]
Honore B, Baandrup U, Nielsen S. et al. Endonuclein is a cell cycle regulated WD-repeat protein that is up-regulated in adenocarcinoma of the pancreas. Oncogene. 2002;21(7):1123–29. [PubMed: 11850830]
Chernova OB, Hunyadi A, Malaj E. et al. A novel member of the WD-repeat gene family, WDR11, maps to the 10q26 region and is disrupted by a chromosome translocation in human glioblastoma cells. Oncogene. 2001;20(38):5378–92. [PubMed: 11536051]
Polakis P. Wnt signaling and cancer. Genes Dev. 2000;14(15):1837–51. [PubMed: 10921899]
Parisi MA, Doherty D, Eckert ML. et al. AHI1 mutations cause both retinal dystrophy and renal cystic disease in Joubert syndrome. J Med Genet. 2006;43(4):334–39. [PMC free article: PMC2563230] [PubMed: 16155189]
Copyright © 2000-2013, Landes Bioscience.
Bookshelf ID: NBK6426


  • PubReader
  • Print View
  • Cite this Page

Related information

  • PMC
    PubMed Central citations
  • PubMed
    Links to PubMed

Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...