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Structural insight into the dimerization of human protein disulfide isomerase
Author(s) -
BastosAristizabal Sara,
Kozlov Guennadi,
Gehring Kalle
Publication year - 2014
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2444
Subject(s) - protein disulfide isomerase , endoplasmic reticulum , isomerase , chemistry , foldase , disulfide bond , isomerization , biophysics , biochemistry , protein folding , stereochemistry , enzyme , biology , catalysis , escherichia coli , groel , gene
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.