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Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity

Protein disulfide isomerase (PDI) supports proinsulin folding as chaperone and isomerase. Here, we focus on how the two PDI functions influence individual steps in the complex folding process of proinsulin. We generated a PDI mutant (PDI-aba′c) where the b′ domain was partially deleted, thus abolish...

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Détails bibliographiques
Auteurs principaux: Winter, Jeannette, Gleiter, Stefan, Klappa, Peter, Lilie, Hauke
Format: Artigo
Langue:Inglês
Publié: Wiley Subscription Services, Inc., A Wiley Company 2011
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC3064837/
https://ncbi.nlm.nih.gov/pubmed/21308844
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.592
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