Wodak, SJ, Paci, E orcid.org/0000-0002-4891-2768, Dokholyan, NV et al. (36 more authors) (2019) Allostery in Its Many Disguises: From Theory to Applications. Structure, 27 (4). pp. 566-578. ISSN 0969-2126
Abstract
Allosteric regulation plays an important role in many biological processes, such as signal transduction, transcriptional regulation, and metabolism. Allostery is rooted in the fundamental physical properties of macromolecular systems, but its underlying mechanisms are still poorly understood. A collection of contributions to a recent interdisciplinary CECAM (Center Européen de Calcul Atomique et Moléculaire) workshop is used here to provide an overview of the progress and remaining limitations in the understanding of the mechanistic foundations of allostery gained from computational and experimental analyses of real protein systems and model systems. The main conceptual frameworks instrumental in driving the field are discussed. We illustrate the role of these frameworks in illuminating molecular mechanisms and explaining cellular processes, and describe some of their promising practical applications in engineering molecular sensors and informing drug design efforts.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2019 Published by Elsevier Ltd. This is an author produced version of a paper published in Structure. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | Allostery; protein conformational changes; regulation; protein function; molecular dynamics; elastic network models; signal transduction; allosteric drugs; allosteric switches; allosteric material; energy landscape |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 27 Feb 2019 11:49 |
Last Modified: | 07 Feb 2020 01:39 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.str.2019.01.003 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:143004 |