Structural insight into the dimerization of human protein disulfide isomerase

被引：17

作者：

Bastos-Aristizabal, Sara ^{[1
]}

Kozlov, Guennadi ^{[1
]}

Gehring, Kalle ^{[1
]}

机构：

[1] McGill Univ, Dept Biochem, Grp Rech Axe Struct Prot, Montreal, PQ H3G 0B1, Canada

来源：

PROTEIN SCIENCE | 2014年 / 23卷 / 05期

基金：

加拿大自然科学与工程研究理事会;

关键词：

crystal structure; thioredoxin-like domain; endoplasmic reticulum; protein disulfide isomerase; dimerization; ENDOPLASMIC-RETICULUM; FAMILY; PDI; DOMAINS; PATHWAY; CELLS;

D O I：

10.1002/pro.2444

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：

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 angstrom 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. PDB Code(s):

引用

页码：618 / 626

页数：9

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