Toward Comprehensive Allosteric Control over Protein Activity

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Toward Comprehensive Allosteric Control over Protein Activity
Title:
Toward Comprehensive Allosteric Control over Protein Activity
Journal Title:
Structure
Publication Date:
28 February 2019
Citation:
Toward Comprehensive Allosteric Control over Protein Activity Guarnera, Enrico et al. Structure, Volume 27, Issue 5, 866 - 878.e1
Abstract:
Universality of allosteric signaling in proteins, molecular machines, and receptors complemented by the great advantages of prospected allosteric drugs in the highly specific, non-competitive, and modulatory nature of their actions calls for deeper theoretical understanding of allosteric communication. We present a computational model that makes it possible to tackle the problem of modulating the energetics of protein allosteric communication. In the context of the energy landscape paradigm, allosteric signaling is always a result of perturbations, such as ligand binding, mutations, and intermolecular interactions. The calculation of local partition functions in the protein harmonic model with perturbations allows us to evaluate the energetics of allosteric communication at the single-residue level. In this framework, Allosteric Signaling Maps are proposed as a tool to exhaustively describe allosteric communication in the protein, to tune already existing signaling, and to design new elements of regulation for taking the protein activity under allosteric control.
License type:
PublisherCopyrights
Funding Info:
This research is supported by core funding from the Bioinformatics Institute, ARES.
Description:
The full paper is available for download at the publisher's URL: https://doi.org/10.1016/j.str.2019.01.014
ISSN:
0969-2126
1878-4186
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