Nuclear magnetic resonance characterization of the...[Protein Sci. 1995]

SearchDatabase nameforSearch term

Advanced Search

Your browser version may not work well with NCBI's Web applications. More information here...

Display Show

All: 1

Review: 0

Click to change filter selection through MyNCBI.

1: Protein Sci. 1995 Dec;4(12):2587-93. Links

Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase.

Kemmink J, Darby NJ, Dijkstra K, Scheek RM, Creighton TE.

European Molecular Biology Laboratory, Heidelberg, Germany.

A genetically engineered protein consisting of the 120 residues at the N-terminus of human protein disulfide isomerase (PDI) has been characterized by 1H, 13C, and 15N NMR methods. The sequence of this protein is 35% identical to Escherichia coli thioredoxin, and it has been found also to have similar patterns of secondary structure and beta-sheet topology. The results confirm that PDI is a modular, multidomain protein. The last 20 residues of the N-terminal domain of PDI are some of those that are similar to part of the estrogen receptor, yet they appear to be an intrinsic part of the thioredoxin fold. This observation makes it unlikely that any of the segments of PDI with similarities to the estrogen receptor comprise individual domains.

PMID: 8580850 [PubMed - indexed for MEDLINE]

PMCID: PMC2143042

Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.
Biochemistry. 1996 Jun 18; 35(24):7684-91.

[Biochemistry. 1996]
The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.
Curr Biol. 1997 Apr 1; 7(4):239-45.

[Curr Biol. 1997]
Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase.
Biochemistry. 1995 Sep 19; 34(37):11725-35.

[Biochemistry. 1995]
ReviewEnzymatic catalysis of disulfide formation.
Protein Expr Purif. 1994 Feb; 5(1):1-13.

[Protein Expr Purif. 1994]
ReviewProtein disulphide isomerase: building bridges in protein folding.
Trends Biochem Sci. 1994 Aug; 19(8):331-6.

[Trends Biochem Sci. 1994]
» See reviews... | » See all...

Cited by 5 PubMed Central articles

Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp.
Ruddock LW, Freedman RB, Klappa P. Protein Sci. 2000 Apr; 9(4):758-64.

[Protein Sci. 2000]
The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.
Koivunen P, Pirneskoski A, Karvonen P, Ljung J, Helaakoski T, Notbohm H, Kivirikko KI. EMBO J. 1999 Jan 4; 18(1):65-74.

[EMBO J. 1999]
Differences between the electronic environments of reduced and oxidized Escherichia coli DsbA inferred from heteronuclear magnetic resonance spectroscopy.
Couprie J, Remerowski ML, Bailleul A, Courçon M, Gilles N, Quéméneur E, Jamin N. Protein Sci. 1998 Oct; 7(10):2065-80.

[Protein Sci. 1998]
» See all...

Structures reported by this article

Human Protein Disulfide Isomerase, Nmr, 40 Structures

PDB: 1MEK

Source: Homo sapiens

Method: Nmr, 40 Structures

Patient Drug Information

Estrogen (Cenestin® , Enjuvia® , Estrace® , ...)
Estrogen is used to treat hot flushes ('hot flashes'; sudden strong feelings of heat and sweating) in women who are experiencing menopause ('change of life', the end of monthly menstrual periods). Some brands of estrogen...
Source: AHFS Consumer Medication Information

Recent Activity

Clear Turn Off Turn On

Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of p...Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase.

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on