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Assisting oxidative protein folding : how do protein disulphide-isomerases couple conformational and chemical processes in protein folding?
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Wallis, A. Katrine and Freedman, R. B. (2013) Assisting oxidative protein folding : how do protein disulphide-isomerases couple conformational and chemical processes in protein folding? In: Topics in Current Chemistry. Springer, pp. 1-34. ISBN 978-3-642-34551-7
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Official URL: http://dx.doi.org/10.1007/128_2011_171
Abstract
Oxidative folding is the simultaneous process of forming disulphide bonds and native structure in proteins. Pathways of oxidative folding are highly diverse and in eukaryotes are catalysed by protein disulphide isomerases (PDIs). PDI consists of four thioredoxin-like domains, two of which contain active sites responsible for disulphide interchange reactions. The four domains are arranged in a horseshoe shape with the two active sites facing each other at the opening of the horseshoe. An extended hydrophobic surface at the bottom of the horseshoe is responsible for non-covalent, hydrophobic interactions with the folding protein. This binding site is capable of distinguishing between fully-folded and partially- or un-folded proteins. PDI is not only a catalyst of the formation of disulphide bonds, but also catalyses folding steps which involve significant conformational change in the folding protein. This review brings together the latest catalytic and structural data aimed at understanding how this is achieved.
Item Type: | Book Item | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | Topics in Current Chemistry | ||||
Publisher: | Springer | ||||
ISBN: | 978-3-642-34551-7 | ||||
ISSN: | 0340-1022 | ||||
Book Title: | Topics in Current Chemistry | ||||
Official Date: | 2013 | ||||
Dates: |
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Volume: | Volume 328 | ||||
Page Range: | pp. 1-34 | ||||
DOI: | 10.1007/128-2011-171 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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