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A structural overview of the PDI family of proteins
Author(s) -
Kozlov Guennadi,
Määttänen Pekka,
Thomas David Y.,
Gehring Kalle
Publication year - 2010
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2010.07793.x
Subject(s) - protein disulfide isomerase , endoplasmic reticulum , protein folding , folding (dsp implementation) , isomerase , disulfide bond , posttranslational modification , chaperone (clinical) , foldase , chemistry , oxidative folding , substrate specificity , microbiology and biotechnology , enzyme , biology , biochemistry , gene , engineering , groel , escherichia coli , medicine , pathology , electrical engineering
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.