Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1699, Issue 1-2, Pages 35-44Publisher
ELSEVIER
DOI: 10.1016/j.bbapap.2004.02.017
Keywords
extracellular protein; protein disulfide isomerase; folding catalyst
Categories
Funding
- NIGMS NIH HHS [T32 GM008280, R01 GM 40379, T32 GM 08280] Funding Source: Medline
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During the maturation of extracellular proteins, disulfide bonds that chemically cross-link specific cysteines are often added to stabilize a protein or to join it covalently to other proteins. Disulfide formation, which requires a change in the covalent structure of the protein, occurs as the protein folds into its three-dimensional structure. In the eukaryotic endoplasmic reticulum and in the bacterial periplasm, an elaborate system of chaperones and folding catalysts ensure that disulfides connect the proper cysteines and that the folding protein does not make improper interactions. This review focuses specifically on one of these folding assistants, protein disulfide isomerase (PDI), an enzyme that catalyzes disulfide formation and isomerization and a chaperone that inhibits aggregation. (C) 2004 Elsevier B.V. All rights reserved.
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