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Protein Sci. Jul 2000; 9(7): 1382–1390.
PMCID: PMC2144677

HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold.


Domains belonging to the immunoglobulin-like fold are responsible for a wide variety of molecular recognition processes. Here we describe a new family of domains, the HYR family, which is predicted to belong to this fold, and which appears to be involved in cellular adhesion. HYR domains were identified in several eukaryotic proteins, often associated with Complement Control Protein (CCP) modules or arranged in multiple copies. Our analysis provides a sequence and structural basis for understanding the role of these domains in interaction mechanisms and leads to further characterization of heretofore undescribed repeated domains with similar folds found in several bacterial proteins involved in enzymatic activities (some chitinases) or in cell surface adhesion (streptococcal C-alpha antigen).

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Selected References

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  • Altschul SF, Koonin EV. Iterated profile searches with PSI-BLAST--a tool for discovery in protein databases. Trends Biochem Sci. 1998 Nov;23(11):444–447. [PubMed]
  • Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997 Sep 1;25(17):3389–3402. [PMC free article] [PubMed]
  • Barlow PN, Steinkasserer A, Norman DG, Kieffer B, Wiles AP, Sim RB, Campbell ID. Solution structure of a pair of complement modules by nuclear magnetic resonance. J Mol Biol. 1993 Jul 5;232(1):268–284. [PubMed]
  • Baron M, Main AL, Driscoll PC, Mardon HJ, Boyd J, Campbell ID. 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin. Biochemistry. 1992 Feb 25;31(7):2068–2073. [PubMed]
  • Bateman A, Birney E, Durbin R, Eddy SR, Finn RD, Sonnhammer EL. Pfam 3.1: 1313 multiple alignments and profile HMMs match the majority of proteins. Nucleic Acids Res. 1999 Jan 1;27(1):260–262. [PMC free article] [PubMed]
  • Bodian DL, Jones EY, Harlos K, Stuart DI, Davis SJ. Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution. Structure. 1994 Aug 15;2(8):755–766. [PubMed]
  • Bork P, Doolittle RF. Proposed acquisition of an animal protein domain by bacteria. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):8990–8994. [PMC free article] [PubMed]
  • Bork P, Downing AK, Kieffer B, Campbell ID. Structure and distribution of modules in extracellular proteins. Q Rev Biophys. 1996 May;29(2):119–167. [PubMed]
  • Bork P, Holm L, Sander C. The immunoglobulin fold. Structural classification, sequence patterns and common core. J Mol Biol. 1994 Sep 30;242(4):309–320. [PubMed]
  • Bycroft M, Bateman A, Clarke J, Hamill SJ, Sandford R, Thomas RL, Chothia C. The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease. EMBO J. 1999 Jan 15;18(2):297–305. [PMC free article] [PubMed]
  • Callebaut I, Courvalin JC, Mornon JP. The BAH (bromo-adjacent homology) domain: a link between DNA methylation, replication and transcriptional regulation. FEBS Lett. 1999 Mar 5;446(1):189–193. [PubMed]
  • Callebaut I, Labesse G, Durand P, Poupon A, Canard L, Chomilier J, Henrissat B, Mornon JP. Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives. Cell Mol Life Sci. 1997 Aug;53(8):621–645. [PubMed]
  • Campbell ID, Spitzfaden C. Building proteins with fibronectin type III modules. Structure. 1994 May 15;2(5):333–337. [PubMed]
  • Choudhury D, Thompson A, Stojanoff V, Langermann S, Pinkner J, Hultgren SJ, Knight SD. X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli. Science. 1999 Aug 13;285(5430):1061–1066. [PubMed]
  • Cuff JA, Clamp ME, Siddiqui AS, Finlay M, Barton GJ. JPred: a consensus secondary structure prediction server. Bioinformatics. 1998;14(10):892–893. [PubMed]
  • Eddy SR. Profile hidden Markov models. Bioinformatics. 1998;14(9):755–763. [PubMed]
  • Gouet P, Courcelle E, Stuart DI, Métoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics. 1999 Apr;15(4):305–308. [PubMed]
  • Halaby DM, Poupon A, Mornon J. The immunoglobulin fold family: sequence analysis and 3D structure comparisons. Protein Eng. 1999 Jul;12(7):563–571. [PubMed]
  • Harpaz Y, Chothia C. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J Mol Biol. 1994 May 13;238(4):528–539. [PubMed]
  • Hofmann K, Bucher P, Falquet L, Bairoch A. The PROSITE database, its status in 1999. Nucleic Acids Res. 1999 Jan 1;27(1):215–219. [PMC free article] [PubMed]
  • Huber AH, Wang YM, Bieber AJ, Bjorkman PJ. Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A. Neuron. 1994 Apr;12(4):717–731. [PubMed]
  • Jones EY. Three-dimensional structure of cell adhesion molecules. Curr Opin Cell Biol. 1996 Oct;8(5):602–608. [PubMed]
  • Jones EY, Harlos K, Bottomley MJ, Robinson RC, Driscoll PC, Edwards RM, Clements JM, Dudgeon TJ, Stuart DI. Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 A resolution. Nature. 1995 Feb 9;373(6514):539–544. [PubMed]
  • Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science. 1992 Nov 6;258(5084):987–991. [PubMed]
  • Little E, Bork P, Doolittle RF. Tracing the spread of fibronectin type III domains in bacterial glycohydrolases. J Mol Evol. 1994 Dec;39(6):631–643. [PubMed]
  • Meindl A, Carvalho MR, Herrmann K, Lorenz B, Achatz H, Lorenz B, Apfelstedt-Sylla E, Wittwer B, Ross M, Meitinger T. A gene (SRPX) encoding a sushi-repeat-containing protein is deleted in patients with X-linked retinitis pigmentosa. Hum Mol Genet. 1995 Dec;4(12):2339–2346. [PubMed]
  • Overduin M, Harvey TS, Bagby S, Tong KI, Yau P, Takeichi M, Ikura M. Solution structure of the epithelial cadherin domain responsible for selective cell adhesion. Science. 1995 Jan 20;267(5196):386–389. [PubMed]
  • Ponting CP, Schultz J, Milpetz F, Bork P. SMART: identification and annotation of domains from signalling and extracellular protein sequences. Nucleic Acids Res. 1999 Jan 1;27(1):229–232. [PMC free article] [PubMed]
  • Reid KB, Day AJ. Structure-function relationships of the complement components. Immunol Today. 1989 Jun;10(6):177–180. [PubMed]
  • Sauer FG, Fütterer K, Pinkner JS, Dodson KW, Hultgren SJ, Waksman G. Structural basis of chaperone function and pilus biogenesis. Science. 1999 Aug 13;285(5430):1058–1061. [PubMed]
  • Shankar V, Baghdayan AS, Huycke MM, Lindahl G, Gilmore MS. Infection-derived Enterococcus faecalis strains are enriched in esp, a gene encoding a novel surface protein. Infect Immun. 1999 Jan;67(1):193–200. [PMC free article] [PubMed]
  • Patel DJ, Gumbiner BM. Cell-cell recognition. Zipping together a cell adhesion interface. Nature. 1995 Mar 23;374(6520):306–307. [PubMed]
  • Shapiro L, Kwong PD, Fannon AM, Colman DR, Hendrickson WA. Considerations on the folding topology and evolutionary origin of cadherin domains. Proc Natl Acad Sci U S A. 1995 Jul 18;92(15):6793–6797. [PMC free article] [PubMed]
  • Stålhammar-Carlemalm M, Areschoug T, Larsson C, Lindahl G. The R28 protein of Streptococcus pyogenes is related to several group B streptococcal surface proteins, confers protective immunity and promotes binding to human epithelial cells. Mol Microbiol. 1999 Jul;33(1):208–219. [PubMed]
  • Suzuki K, Taiyoji M, Sugawara N, Nikaidou N, Henrissat B, Watanabe T. The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases. Biochem J. 1999 Nov 1;343(Pt 3):587–596. [PMC free article] [PubMed]
  • Wästfelt M, Stâlhammar-Carlemalm M, Delisse AM, Cabezon T, Lindahl G. Identification of a family of streptococcal surface proteins with extremely repetitive structure. J Biol Chem. 1996 Aug 2;271(31):18892–18897. [PubMed]
  • Wessel GM, Berg L, Adelson DL, Cannon G, McClay DR. A molecular analysis of hyalin--a substrate for cell adhesion in the hyaline layer of the sea urchin embryo. Dev Biol. 1998 Jan 15;193(2):115–126. [PubMed]

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