Department of Biochemistry, McGill University, Montréal, Québec, Canada.
FEBS J. 2010 Oct;277(19):3924-36. doi: 10.1111/j.1742-4658.2010.07793.x. Epub 2010 Aug 26.
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.
蛋白质二硫键异构酶(PDI)是在内质网中介导氧化蛋白折叠的酶。由于缺乏结构信息,PDI 的理解一直受到阻碍。在过去的几年中,PDI 的部分和全长结构以越来越快的速度得到解决。对这些结构的分析揭示了几个最著名的 PDI 家族成员所共有的共同特征,以及与底物和伴侣结合位点相关的独特特征。这些令人兴奋的突破为深入了解细胞中氧化蛋白折叠的机制提供了帮助。