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.

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
• Public URL: https://durham-repository.worktribe.com/output/1414517