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2013 | OriginalPaper | Buchkapitel

Assisting Oxidative Protein Folding: How Do Protein Disulphide-Isomerases Couple Conformational and Chemical Processes in Protein Folding?

verfasst von : A. Katrine Wallis, Robert B. Freedman

Erschienen in: Molecular Chaperones

Verlag: Springer Berlin Heidelberg

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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.

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Nächstes Kapitel Peptide Bond cis/trans Isomerases: A Biocatalysis Perspective of Conformational Dynamics in Proteins
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Metadaten
Titel
Assisting Oxidative Protein Folding: How Do Protein Disulphide-Isomerases Couple Conformational and Chemical Processes in Protein Folding?
verfasst von
A. Katrine Wallis
Robert B. Freedman
Copyright-Jahr
2013
Verlag
Springer Berlin Heidelberg
Buch
Molecular Chaperones

Print ISBN: 978-3-642-34551-7

Electronic ISBN: 978-3-642-34552-4

Copyright-Jahr: 2013

DOI
https://doi.org/10.1007/128_2011_171