人蛋白二硫键异构酶二聚化结构的研究进展
Structural insight into the dimerization of human protein disulfide isomerase.
机构信息
Department of Biochemistry, Groupe de recherche axé sur la structure des protéines, McGill University, 3649 Promenade Sir William Osler, Montréal, Québec, H3G 0B1, Canada.
出版信息
Protein Sci. 2014 May;23(5):618-26. doi: 10.1002/pro.2444. Epub 2014 Mar 11.
Abstract
Protein disulfide isomerases (PDIs) are responsible for catalyzing the proper oxidation and isomerization of disulfide bonds of newly synthesized proteins in the endoplasmic reticulum (ER). Here, it is shown that human PDI (PDIA1) dimerizes in vivo and proposed that the dimerization of PDI has physiological relevance by autoregulating its activity. The crystal structure of the dimeric form of noncatalytic bb' domains of human PDIA1 determined to 2.3 Å resolution revealed that the formation of dimers occludes the substrate binding site and may function as a mechanism to regulate PDI activity in the ER.
摘要
蛋白质二硫键异构酶（PDI）负责催化内质网（ER）中新合成蛋白质中二硫键的正确氧化和异构化。本文显示，人 PDI（PDIA1）在体内二聚化，并提出 PDI 的二聚化通过自身调节其活性具有生理相关性。人 PDIA1 的非催化 bb'结构域二聚体的晶体结构在 2.3 Å 分辨率下确定，揭示了二聚体的形成会阻塞底物结合位点，并且可能作为一种调节 ER 中 PDI 活性的机制。
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