The ensemble nature of allostery

Allostery is the process by which biological macromolecules transmit the effect of binding at one site to another, often distal, functional site, allowing for the regulation of activity; here facilitation of allostery through dynamic and intrinsically disordered proteins is discussed, and a framewor...

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Published in	Nature (London) Vol. 508; no. 7496; pp. 331 - 339
Main Authors	Motlagh, Hesam N., Wrabl, James O., Li, Jing, Hilser, Vincent J.
Format	Journal Article
Language	English
Published	London Nature Publishing Group UK 17.04.2014 Nature Publishing Group
Subjects	631/45 631/57 Allosteric proteins Allosteric Regulation Allosteric Site Binding sites Biological research Biology Biology, Experimental Chemical properties Cooperative binding (Biochemistry) Hemoglobins - chemistry Hemoglobins - metabolism Humanities and Social Sciences Ligands Models, Molecular multidisciplinary Protein Unfolding Proteins Proteins - chemistry Proteins - metabolism review-article Science Structure Thermodynamics United States
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Abstract	Allostery is the process by which biological macromolecules transmit the effect of binding at one site to another, often distal, functional site, allowing for the regulation of activity; here facilitation of allostery through dynamic and intrinsically disordered proteins is discussed, and a framework to unify the description of allosteric mechanisms for different systems is proposed. The changing shape of allostery The classic model for understanding allostery, the regulated process by which biological macromolecules (typically enzymes) transmit the effect of binding at one site to another with subsequent change in activity, has focused on unique structures and the structural changes observed between different functional forms. During the past 20 years there has been a realization that allostery is associated with changes in dynamics as well. In this Review, Vincent Hilser and colleagues discuss how allostery can be facilitated by dynamic and intrinsically disordered proteins and propose a framework to unify the description of allosteric mechanisms from different systems. Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional site, allowing for regulation of activity. Recent experimental observations demonstrating that allostery can be facilitated by dynamic and intrinsically disordered proteins have resulted in a new paradigm for understanding allosteric mechanisms, which focuses on the conformational ensemble and the statistical nature of the interactions responsible for the transmission of information. Analysis of allosteric ensembles reveals a rich spectrum of regulatory strategies, as well as a framework to unify the description of allosteric mechanisms from different systems.
AbstractList	Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional site, allowing for regulation of activity. Recent experimental observations demonstrating that allostery can be facilitated by dynamic and intrinsically disordered proteins have resulted in a new paradigm for understanding allosteric mechanisms, which focuses on the conformational ensemble and the statistical nature of the interactions responsible for the transmission of information. Analysis of allosteric ensembles reveals a rich spectrum of regulatory strategies, as well as a framework to unify the description of allosteric mechanisms from different systems. Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional site, allowing for regulation of activity. Recent experimental observations demonstrating that allostery can be facilitated by dynamic and intrinsically disordered proteins have resulted in a new paradigm for understanding allosteric mechanisms, which focuses on the conformational ensemble and the statistical nature of the interactions responsible for the transmission of information. Analysis of allosteric ensembles reveals a rich spectrum of regulatory strategies, as well as a framework to unify the description of allosteric mechanisms from different systems. [PUBLICATION ABSTRACT] Allostery is the process by which biological macromolecules transmit the effect of binding at one site to another, often distal, functional site, allowing for the regulation of activity; here facilitation of allostery through dynamic and intrinsically disordered proteins is discussed, and a framework to unify the description of allosteric mechanisms for different systems is proposed. The changing shape of allostery The classic model for understanding allostery, the regulated process by which biological macromolecules (typically enzymes) transmit the effect of binding at one site to another with subsequent change in activity, has focused on unique structures and the structural changes observed between different functional forms. During the past 20 years there has been a realization that allostery is associated with changes in dynamics as well. In this Review, Vincent Hilser and colleagues discuss how allostery can be facilitated by dynamic and intrinsically disordered proteins and propose a framework to unify the description of allosteric mechanisms from different systems. Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional site, allowing for regulation of activity. Recent experimental observations demonstrating that allostery can be facilitated by dynamic and intrinsically disordered proteins have resulted in a new paradigm for understanding allosteric mechanisms, which focuses on the conformational ensemble and the statistical nature of the interactions responsible for the transmission of information. Analysis of allosteric ensembles reveals a rich spectrum of regulatory strategies, as well as a framework to unify the description of allosteric mechanisms from different systems.
Audience	Academic
Author	Hilser, Vincent J. Li, Jing Motlagh, Hesam N. Wrabl, James O.
AuthorAffiliation	1 Department of Biology and T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA
AuthorAffiliation_xml	– name: 1 Department of Biology and T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA
Author_xml	– sequence: 1 givenname: Hesam N. surname: Motlagh fullname: Motlagh, Hesam N. organization: Department of Biology and T.C. Jenkins Department of Biophysics, Johns Hopkins University – sequence: 2 givenname: James O. surname: Wrabl fullname: Wrabl, James O. organization: Department of Biology and T.C. Jenkins Department of Biophysics, Johns Hopkins University – sequence: 3 givenname: Jing surname: Li fullname: Li, Jing organization: Department of Biology and T.C. Jenkins Department of Biophysics, Johns Hopkins University – sequence: 4 givenname: Vincent J. surname: Hilser fullname: Hilser, Vincent J. email: Hilser@jhu.edu organization: Department of Biology and T.C. Jenkins Department of Biophysics, Johns Hopkins University
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/24740064$$D View this record in MEDLINE/PubMed
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Snippet	Allostery is the process by which biological macromolecules transmit the effect of binding at one site to another, often distal, functional site, allowing for... Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional...
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SubjectTerms	631/45 631/57 Allosteric proteins Allosteric Regulation Allosteric Site Binding sites Biological research Biology Biology, Experimental Chemical properties Cooperative binding (Biochemistry) Hemoglobins - chemistry Hemoglobins - metabolism Humanities and Social Sciences Ligands Models, Molecular multidisciplinary Protein Unfolding Proteins Proteins - chemistry Proteins - metabolism review-article Science Structure Thermodynamics
Title	The ensemble nature of allostery
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