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Free Radic Biol Med. 2015 Jun;83:305-13. doi: 10.1016/j.freeradbiomed.2015.02.007. Epub 2015 Feb 17.

Protein disulfide-isomerase, a folding catalyst and a redox-regulated chaperone.

Author information

1
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
2
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. Electronic address: chihwang@sun5.ibp.ac.cn.

Abstract

Protein disulfide-isomerase (PDI) 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.

KEYWORDS:

Chaperone; Endoplasmic reticulum; Oxidative protein folding; Protein conformation; Protein disulfideā€“isomerise; Redox regulation

[Indexed for MEDLINE]

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