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

2013 | OriginalPaper | Buchkapitel

Allostery in the Hsp70 Chaperone Proteins

verfasst von : Erik R. P. Zuiderweg, Eric B. Bertelsen, Aikaterini Rousaki, Matthias P. Mayer, Jason E. Gestwicki, Atta Ahmad

Erschienen in: Molecular Chaperones

Verlag: Springer Berlin Heidelberg

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Abstract

Heat shock 70-kDa (Hsp70) chaperones are essential to in vivo protein folding, protein transport, and protein re-folding. They carry out these activities using repeated cycles of binding and release of client proteins. This process is under allosteric control of nucleotide binding and hydrolysis. X-ray crystallography, NMR spectroscopy, and other biophysical techniques have contributed much to the understanding of the allosteric mechanism linking these activities and the effect of co-chaperones on this mechanism. In this chapter these findings are critically reviewed. Studies on the allosteric mechanisms of Hsp70 have gained enhanced urgency, as recent studies have implicated this chaperone as a potential drug target in diseases such as Alzheimer’s and cancer. Recent approaches to combat these diseases through interference with the Hsp70 allosteric mechanism are discussed.

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Vorheriges Kapitel Small Heat-Shock Proteins: Paramedics of the Cell
Nächstes Kapitel Hsp90: Structure and Function
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Metadaten
Titel
Allostery in the Hsp70 Chaperone Proteins
verfasst von
Erik R. P. Zuiderweg
Eric B. Bertelsen
Aikaterini Rousaki
Matthias P. Mayer
Jason E. Gestwicki
Atta Ahmad
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_2012_323