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Global low-frequency motions in protein allostery: CAP as a model system

Townsend, P.D.; Rogers, T.L.; Pohl, E.; Wilson, M.R.; McLeish, T.C.B.; Cann, M.J.

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Authors

P.D. Townsend

T.L. Rogers

T.C.B. McLeish



Abstract

Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of Escherichia coli is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding.

Citation

Townsend, P., Rogers, T., Pohl, E., Wilson, M., McLeish, T., & Cann, M. (2015). Global low-frequency motions in protein allostery: CAP as a model system. Biophysical Reviews, 7(2), 175-182. https://doi.org/10.1007/s12551-015-0163-9

Journal Article Type Article
Acceptance Date Jan 12, 2015
Online Publication Date Feb 4, 2015
Publication Date Jun 1, 2015
Deposit Date Jan 13, 2015
Publicly Available Date Feb 11, 2015
Journal Biophysical Reviews
Print ISSN 1867-2450
Electronic ISSN 1867-2469
Publisher Springer
Peer Reviewed Peer Reviewed
Volume 7
Issue 2
Pages 175-182
DOI https://doi.org/10.1007/s12551-015-0163-9
Keywords Protein, Allostery, Dynamics, Catabolite activator protein, Normal modes, Elastic network model

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Copyright Statement
Advance online version © The Author(s) 2015. This article is published with open access at Springerlink.com. Open Access. This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.








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