Cross-strand disulfides in the non-hydrogen bonding site of antiparallel β-sheet (aCSDns): poised for biological switching
Author:
Affiliation:
1. Life and Environmental Sciences
2. Deakin University
3. Geelong 3217
4. Australia
5. Victor Chang Cardiac Research Institute
6. Olivia Newton-John Cancer Research Institute
7. Heidelberg 3084
8. School of Cancer Medicine
9. La Trobe University
Abstract
aCSDns are forbidden disulfides with protein redox-activity. Within the aCSDn structural motif, a cognate substrate of Trx-like enzymes, the disulfide bonds are strained and metastable, facilitating their role as redox-regulated protein switches.
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2015/RA/C5RA10672A
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