Ontology highlight
ABSTRACT:
SUBMITTER: Wang C
PROVIDER: S-EPMC3256865 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20111116 2
Protein-disulfide isomerase (PDI), with domains arranged as abb'xa'c, is a key enzyme and chaperone localized in the endoplasmic reticulum (ER) catalyzing oxidative folding and preventing misfolding/aggregation of proteins. It has been controversial whether the chaperone activity of PDI is redox-regulated, and the molecular basis is unclear. Here, we show that both the chaperone activity and the overall conformation of human PDI are redox-regulated. We further demonstrate that the conformational ...[more]