Protein disulfide isomerases exploit synergy between catalytic and specific binding domains

EMBO Reports

Volumn 3, Issue 2, 2002, Pages 136-140

  Freedman, Robert B ^a   Klappa, Peter ^a   Ruddock, Lloyd W ^b  

^a UNIVERSITY OF KENT   (United Kingdom)

^b UNIVERSITY OF OULU   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; PEPTIDE; POLYPEPTIDE; PROTEIN DISULFIDE ISOMERASE; THIOL;

ARTICLE; BINDING SITE; CATALYSIS; CATALYST; CHEMICAL REACTION; CONTROLLED STUDY; DISULFIDE BOND; HUMAN; ISOMERISM; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN STRUCTURE; STRUCTURAL HOMOLOGY;

ANIMALS; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; HUMANS; OXIDOREDUCTASES; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; THIOREDOXIN;

EID: 0036198797     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1093/embo-reports/kvf035     Document Type: Article

References (49)

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6. Functional-properties of the individual thioredoxin-like domains of protein disulfide-isomerase
7. The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency
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14. Experimental and theoretical analyses of the domain architecture of mammalian protein disulfide-isomerase
15. A molecular model for the redox potential differences between thioredoxin and DsbA based on electrostatic calculations
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17. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
18. Native and non-native intermediates in the BPTI folding pathway
19. Why is DsbA such an oxidising disulfide catalyst?
20. Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family
21. Molecular-cloning of the cDNA-encoding a novel protein disulfide isomerase-related protein (PDIr)
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24. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
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26. Interactions between protein disulfide isomerase and peptides
27. The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
28. A pancreas-specific glycosylated protein disulfide-isomerase binds to misfolded proteins and peptides with an interaction inhibited by oestrogens
29. The pancreas-specific protein disulfide-isomerase PDIp interacts with a hydroxyaryl group in ligands
30. ER60/ERp57 forms disulfide-bonded intermediates with MHC class I heavy chain
31. Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: Comparison with protein disulfide isomerase
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34. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase
35. Thiol-independent interaction of protein disulfide isomerase with type X collagen during intra-cellular folding and assembly
36. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
37. Domains b′ and a′ of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase: The N-terminal domains a and b enhance this and can be substituted in part by those of ERp57
38. Specificity in substrate binding by protein folding catalysts: Tyrosine and tryptophan residues are recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp
39. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding
40. Chaperone-like activity of protein disulfide-isomerase in the refolding of modanese
41. Site-directed mutagenesis of human protein disulfide isomerase: Effect on the assembly, activity and endoplasmic reticulum retention of human prolyl-4-hydroxylase in Spodoptera frugiperda insect cells
42. The enzymatic and non-enzymatic roles of protein-disulfide isomerase in apolipoprotein B secretion
43. Interaction of the periplasmic peptidyl-prolyl cis-trans isomerase SurA with model peptides: The N-terminus of SurA is essential for peptide binding
44. Efficient catalysis of disulfide bond rearrangements by protein disulfide-isomerase
45. Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein
46. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
47. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
48. Modular structure of the trigger factor required for high activity in protein folding