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Replacement of domain b of human protein disulfide isomerase-related protein with domain b′ of human protein disulfide isomerase dramatically increases its chaperone activity

✍ Scribed by Tomohisa Horibe; Daisuke Iguchi; Toshio Masuoka; Mitsuhiro Gomi; Taiji Kimura; Masakazu Kikuchi

Book ID
116464390
Publisher
Elsevier Science
Year
2004
Tongue
English
Weight
139 KB
Volume
566
Category
Article
ISSN
0014-5793

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Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity
✍ Jeannette Winter; Stefan Gleiter; Peter Klappa; Hauke Lilie 📂 Article 📅 2011 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 715 KB

## Abstract 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 dele