Journal
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
Volume 43, Issue 8, Pages 1079-1085Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biocel.2011.04.002
Keywords
Thiol-based redox regulation; Conformation change; Nitrosylation; Nitrosation; Glutathionylation; Redox-active disulfide; Intrinsically disordered sequences
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Funding
- Australian Partnership for Advanced Computing (APAC) National Facility, the APAC Australian Centre for Advanced Computing and Communications
- NHMRC [459406]
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Cysteine residues in proteins are covalently modified under conditions of oxidative and nitrosative stress by oxidation, nitrosation, glutathionylation and disulfide formation. Modifications induce conformational changes in substrate proteins, effecting signal cascades that evoke a biological response. A growing number of structures with modified cysteines are allowing a piecemeal understanding of the mechanistic aspects of these signalling pathways to emerge. Conformational changes upon conjugation of nitric oxide and glutathione are generally small and often accompanied by a local increase in protein disorder. Burial of nitric oxide is also apparent, which may increase the timeframe of signalling. Conformational changes upon disulfide formation/reduction range from the small to the spectacular. They include order/disorder transitions; oxidation of disulfides following expulsion of metals such as Zn; major reorganisation or morphing of portions of the polypeptide backbone; and changes in quaternary structure including domain swapping. Crown Copyright (C) 2011 Published by Elsevier Ltd. All rights reserved.
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