Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains

Protein kinase A (PKA) is a cyclic nucleotide dependent protein kinase. Here the authors use single molecule optical tweezers and steered molecular dynamic simulations to follow in real time and quantitatively characterize the signals transduced by cAMP through the structure of the PKA regulatory su...

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Autores principales:	Yuxin Hao, Jeneffer P. England, Luca Bellucci, Emanuele Paci, H. Courtney Hodges, Susan S. Taylor, Rodrigo A. Maillard
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e6d9e9b414f34aa48cefa8fdd15dd057
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spelling	oai:doaj.org-article:e6d9e9b414f34aa48cefa8fdd15dd0572021-12-02T16:57:35ZActivation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains10.1038/s41467-019-11930-22041-1723https://doaj.org/article/e6d9e9b414f34aa48cefa8fdd15dd0572019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11930-2https://doaj.org/toc/2041-1723Protein kinase A (PKA) is a cyclic nucleotide dependent protein kinase. Here the authors use single molecule optical tweezers and steered molecular dynamic simulations to follow in real time and quantitatively characterize the signals transduced by cAMP through the structure of the PKA regulatory subunit, and propose a model for PKA allosteric activation.Yuxin HaoJeneffer P. EnglandLuca BellucciEmanuele PaciH. Courtney HodgesSusan S. TaylorRodrigo A. MaillardNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yuxin Hao Jeneffer P. England Luca Bellucci Emanuele Paci H. Courtney Hodges Susan S. Taylor Rodrigo A. Maillard Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains
description	Protein kinase A (PKA) is a cyclic nucleotide dependent protein kinase. Here the authors use single molecule optical tweezers and steered molecular dynamic simulations to follow in real time and quantitatively characterize the signals transduced by cAMP through the structure of the PKA regulatory subunit, and propose a model for PKA allosteric activation.
format	article
author	Yuxin Hao Jeneffer P. England Luca Bellucci Emanuele Paci H. Courtney Hodges Susan S. Taylor Rodrigo A. Maillard
author_facet	Yuxin Hao Jeneffer P. England Luca Bellucci Emanuele Paci H. Courtney Hodges Susan S. Taylor Rodrigo A. Maillard
author_sort	Yuxin Hao
title	Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains
title_short	Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains
title_full	Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains
title_fullStr	Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains
title_full_unstemmed	Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains
title_sort	activation of pka via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/e6d9e9b414f34aa48cefa8fdd15dd057
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Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains

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