Protein disulfide isomerase a multifunctional protein with multiple physiological roles

Protein disulfide isomerase (PDI), is a member of the thioredoxin superfamily of redox proteins. PDI has three catalytic activities including, thiol-disulfide oxireductase, disulfide isomerase and redox-dependent chaperone. Originally, PDI was identified in the lumen of the endoplasmic reticulum and...

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Veröffentlicht in:Frontiers in chemistry 2014-01, Vol.2, p.70-70
Hauptverfasser: Ali Khan, Hyder, Mutus, Bulent
Format: Artikel
Sprache:eng
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Zusammenfassung:Protein disulfide isomerase (PDI), is a member of the thioredoxin superfamily of redox proteins. PDI has three catalytic activities including, thiol-disulfide oxireductase, disulfide isomerase and redox-dependent chaperone. Originally, PDI was identified in the lumen of the endoplasmic reticulum and subsequently detected at additional locations, such as cell surfaces and the cytosol. This review will provide an overview of the recent advances in relating the structural features of PDI to its multiple catalytic roles as well as its physiological and pathophysiological functions related to redox regulation and protein folding.
ISSN:2296-2646
2296-2646
DOI:10.3389/fchem.2014.00070