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Between-strand disulfides: Forbidden disulfides linking adjacent ß-Strands

Haworth, Naomi L and Wouters, Merridee A 2013, Between-strand disulfides: Forbidden disulfides linking adjacent ß-Strands, RSC Advances, vol. 3, no. 46, pp. 24680-24705.

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Title Between-strand disulfides: Forbidden disulfides linking adjacent ß-Strands
Author(s) Haworth, Naomi L
Wouters, Merridee A
Journal name RSC Advances
Volume number 3
Issue number 46
Start page 24680
End page 24705
Total pages 26
Publisher RSC Publishing
Place of publication Cambridge, UK
Publication date 2013
ISSN 2046-2069
Keyword(s) Redox-active disulfide
Forbidden disulfide
Disulfide reduction
Disulfide
Redox reactions
Summary Between-strand disulfides (BSDs) connect cysteine (Cys) residues across adjacent strands of β-sheets. There are four BSD types which can be found in regular β-structure: CSDs, which link residues immediately opposite each other in the β-structure (residues i and j); ETDs, which connect Cys out of register by one residue (i and j ± 1); BDDs, which join Cys at positions i and j ± 2; and BFDs, which link residues i and j ± 3. Formation of these disulfides was initially predicted to be forbidden, producing too much local strain in the protein fold. However, BSDs do exist in nature. Significantly, their high levels of strain allow them to be involved in redox processes under physiological conditions. Here we characterise BSD motifs found in the Protein Data Bank (PDB), discussing important intrinsic factors, such as the disulfide conformation and torsional strain, and extrinsic factors, such as the influence of the β-sheet environment on the disulfide and vice versa. We also discuss the biological importance of BSDs, including the prevalence of non-homologous examples in the PDB, the conservation of BSD motifs amongst related proteins (BSD clusters) and experimental evidence for BSD redox activity. For clusters of homologous BSDs we present detailed data of the disulfide properties and the variations of these properties amongst the “redundant” structures. Identification of disulfides with the potential to be involved in biological redox processes via the analysis of these data will provide important insights into the function and mechanism of BSD-containing proteins. Characterisation of thiol-based redox signalling pathways will lead to significant breakthroughs in understanding the molecular basis of oxidative stress and associated pathways, such as ageing and neurodegenerative diseases.
Language eng
Field of Research 060102 Bioinformatics
060112 Structural Biology (incl Macromolecular Modelling)
030701 Quantum Chemistry
Socio Economic Objective 920104 Diabetes
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2013, RSC Publishing
Persistent URL http://hdl.handle.net/10536/DRO/DU:30057393

Document type: Journal Article
Collections: School of Medicine
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Created: Tue, 05 Nov 2013, 10:46:17 EST by Merridee Wouters

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.