Journal
FEBS JOURNAL
Volume 277, Issue 19, Pages 3924-3936Publisher
WILEY
DOI: 10.1111/j.1742-4658.2010.07793.x
Keywords
disulfide; endoplasmic reticulum; ERp44; ERp57; ERp72; PDI; protein folding; protein structure; thioredoxin-like; X-ray crystallography
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Funding
- Canadian Institutes of Health Research
- Fonds de la Recherche en Sante de Quebec
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Protein disulfide isomerases (PDIs) are enzymes that mediate oxidative protein folding in the endoplasmic reticulum. Understanding of PDIs has historically been hampered by lack of structural information. Over the last several years, partial and full-length PDI structures have been solved at an increasing rate. Analysis of the structures reveals common features shared by several of the best known PDI family members, and also unique features related to substrate and partner binding sites. These exciting breakthroughs provide a deeper understanding of the mechanisms of oxidative protein folding in cells.
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