Allostery is one of the cornerstones of biological function, as it plays a fundamental role in regulating protein activity. The modelling of allostery has gradually moved from a conformation-based framework, linked to structural changes, to dynamics-based allostery, whereby the effects of ligand binding propagate via signal transduction from the allosteric site to other regions of the protein via inter-residue interactions. Characterising such allosteric signalling pathways, which do not necessarily lead to conformational changes, has been pursued experimentally and complemented by computational analysis of protein networks to detect subtle dynamic propagation paths. Considering allostery from the perspective of signal transduction broadens the understanding of allosteric mechanisms, underscores the importance of protein topology, and can provide insights into allosteric drug design. Copyright © 2023 The Author(s). Published by Elsevier Ltd.. All rights reserved.
Nan Wu, Mauricio Barahona, Sophia N Yaliraki. Allosteric communication and signal transduction in proteins. Current opinion in structural biology. 2024 Feb;84:102737
PMID: 38171189
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