How Proteins Form Disulfide Bonds

被引：149

作者：

Depuydt, Matthieu ^{[1
,2
]}

Messens, Joris ^{[2
,3
,4
]}

Collet, Jean-Francois ^{[1
,2
]}

机构：

[1] Catholic Univ Louvain, de Duve Inst, B-1200 Brussels, Belgium

[2] Brussels Ctr Redox Biol, Brussels, Belgium

[3] Vlaams Inst Biotechnol, Dept Mol & Cellular Interact, Brussels, Belgium

[4] Vrije Univ Brussel, Brussels, Belgium

来源：

ANTIOXIDANTS & REDOX SIGNALING | 2011年 / 15卷 / 01期

关键词：

MITOCHONDRIAL INTERMEMBRANE SPACE; K EPOXIDE REDUCTASE; THIOREDOXIN-LIKE DOMAIN; GRAM-POSITIVE BACTERIA; CYTOCHROME-C SYNTHESIS; ESCHERICHIA-COLI DSBC; FORMATION IN-VIVO; ENDOPLASMIC-RETICULUM; CRYSTAL-STRUCTURE; ACTIVE-SITE;

D O I：

10.1089/ars.2010.3575

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the study of oxidative protein folding. Oxidative protein folding refers to the composite process by which a protein recovers both its native structure and its native disulfide bonds. Pathways that form disulfide bonds have now been unraveled in the bacterial periplasm (disulfide bond protein A [DsbA], DsbB, DsbC, DsbG, and DsbD), the endoplasmic reticulum (protein disulfide isomerase and Ero1), and the mitochondrial intermembrane space (Mia40 and Erv1). This review summarizes the current knowledge on disulfide bond formation in both prokaryotes and eukaryotes and highlights the major problems that remain to be solved. Antioxid. Redox Signal. 15, 49-66.

引用

页码：49 / 66

页数：18

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