Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 83, Issue -, Pages 305-313Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2015.02.007
Keywords
Chaperone; Endoplasmic reticulum; Oxidative protein folding; Protein conformation; Protein disulfide-isomerise; Redox regulation
Funding
- Chinese Ministry of Science and Technology [2011CB910303, 2012CB911002]
- National Natural Science Foundation of China [31370775, 31370758]
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Protein disulfide-isomerase (PIN) was the first protein-folding catalyst to be characterized, half a century ago. It plays critical roles in a variety of physiological events by displaying oxidoreductase and redox-regulated chaperone activities. This review provides a brief history of the identification of PDI as both an enzyme and a molecular chaperone and of the recent advances in studies on the structure and dynamics of PDI, the substrate binding and release, and the cooperation with its partners to catalyze oxidative protein folding and maintain ER redox homeostasis. In this review, we highlight the structural features of PDI, including the high interdomain flexibility, the multiple binding sites, the two synergic active sites, and the redox-dependent conformational changes. (C) 2015 Elsevier Inc. All rights reserved.
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