Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle

Allosteric interactions are an important contributor to the catalytic properties of enzyme. Here the authors demonstrate—using the prototypical protein kinase PKA—that the allosteric cooperativity underscoring substrate recognition and product release are directly linked to changes in conformational...

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Autores principales:	Yingjie Wang, Manu V.S., Jonggul Kim, Geoffrey Li, Lalima G. Ahuja, Philip Aoto, Susan S. Taylor, Gianluigi Veglia
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a90cc9d95e104b5fb722e046152a3c4e
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spelling	oai:doaj.org-article:a90cc9d95e104b5fb722e046152a3c4e2021-12-02T17:01:26ZGlobally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle10.1038/s41467-019-08655-72041-1723https://doaj.org/article/a90cc9d95e104b5fb722e046152a3c4e2019-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-08655-7https://doaj.org/toc/2041-1723Allosteric interactions are an important contributor to the catalytic properties of enzyme. Here the authors demonstrate—using the prototypical protein kinase PKA—that the allosteric cooperativity underscoring substrate recognition and product release are directly linked to changes in conformational entropy.Yingjie WangManu V.S.Jonggul KimGeoffrey LiLalima G. AhujaPhilip AotoSusan S. TaylorGianluigi VegliaNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yingjie Wang Manu V.S. Jonggul Kim Geoffrey Li Lalima G. Ahuja Philip Aoto Susan S. Taylor Gianluigi Veglia Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle
description	Allosteric interactions are an important contributor to the catalytic properties of enzyme. Here the authors demonstrate—using the prototypical protein kinase PKA—that the allosteric cooperativity underscoring substrate recognition and product release are directly linked to changes in conformational entropy.
format	article
author	Yingjie Wang Manu V.S. Jonggul Kim Geoffrey Li Lalima G. Ahuja Philip Aoto Susan S. Taylor Gianluigi Veglia
author_facet	Yingjie Wang Manu V.S. Jonggul Kim Geoffrey Li Lalima G. Ahuja Philip Aoto Susan S. Taylor Gianluigi Veglia
author_sort	Yingjie Wang
title	Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle
title_short	Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle
title_full	Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle
title_fullStr	Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle
title_full_unstemmed	Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle
title_sort	globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/a90cc9d95e104b5fb722e046152a3c4e
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_version_	1718382166585376768

Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle

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