Protein disulfide-isomerase, a folding catalyst and a redox-regulated chaperone
Protein disulfide-isomerase, a folding catalyst and a redox-regulated chaperone
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蛋白质二硫键异构酶、折叠催化剂和氧化还原调节分子伴侣
DOI：
10.1016/j.freeradbiomed.2015.02.007
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发表时间：
2015-06-01
影响因子：
7.4
通讯作者：
Wang, Chih-chen
中科院分区：
文献类型：
--
作者：
Wang, Lei;Wang, Xi;Wang, Chih-chen
蛋白质二硫键异构酶(PIN)是半个世纪前第一个被表征的蛋白质折叠催化剂。它通过显示氧化还原酶和氧化还原调节的伴侣活性，在多种生理事件中发挥关键作用。本文简要回顾了PDI作为一种酶和分子伴侣的鉴定历史，以及PDI的结构和动力学、底物的结合和释放以及与其合作伙伴在催化蛋白质氧化折叠和维持内质网氧化还原动态平衡方面的最新进展。在这篇综述中，我们重点介绍了PDI的结构特征，包括高度的结构域间灵活性，多个结合位点，两个协同活性位点，以及依赖于氧化还原的构象变化。(C)2015 Elsevier Inc.保留所有权利。
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.