Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding

AMPK regulates the metabolism and so drugs that activate AMPK might have potential for the treatment of metabolic disease. Here, the authors report the structure of AMPK bound to an activating compound, revealing two binding sites and indicating that dual therapy might be a good drug strategy.

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Autores principales:	Christopher G. Langendorf, Kevin R. W. Ngoei, John W. Scott, Naomi X. Y. Ling, Sam M. A. Issa, Michael A. Gorman, Michael W. Parker, Kei Sakamoto, Jonathan S. Oakhill, Bruce E. Kemp
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/750524f5495343399d0ec23522953a11
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spelling	oai:doaj.org-article:750524f5495343399d0ec23522953a112021-12-02T14:40:14ZStructural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding10.1038/ncomms109122041-1723https://doaj.org/article/750524f5495343399d0ec23522953a112016-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms10912https://doaj.org/toc/2041-1723AMPK regulates the metabolism and so drugs that activate AMPK might have potential for the treatment of metabolic disease. Here, the authors report the structure of AMPK bound to an activating compound, revealing two binding sites and indicating that dual therapy might be a good drug strategy.Christopher G. LangendorfKevin R. W. NgoeiJohn W. ScottNaomi X. Y. LingSam M. A. IssaMichael A. GormanMichael W. ParkerKei SakamotoJonathan S. OakhillBruce E. KempNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Christopher G. Langendorf Kevin R. W. Ngoei John W. Scott Naomi X. Y. Ling Sam M. A. Issa Michael A. Gorman Michael W. Parker Kei Sakamoto Jonathan S. Oakhill Bruce E. Kemp Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding
description	AMPK regulates the metabolism and so drugs that activate AMPK might have potential for the treatment of metabolic disease. Here, the authors report the structure of AMPK bound to an activating compound, revealing two binding sites and indicating that dual therapy might be a good drug strategy.
format	article
author	Christopher G. Langendorf Kevin R. W. Ngoei John W. Scott Naomi X. Y. Ling Sam M. A. Issa Michael A. Gorman Michael W. Parker Kei Sakamoto Jonathan S. Oakhill Bruce E. Kemp
author_facet	Christopher G. Langendorf Kevin R. W. Ngoei John W. Scott Naomi X. Y. Ling Sam M. A. Issa Michael A. Gorman Michael W. Parker Kei Sakamoto Jonathan S. Oakhill Bruce E. Kemp
author_sort	Christopher G. Langendorf
title	Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding
title_short	Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding
title_full	Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding
title_fullStr	Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding
title_full_unstemmed	Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding
title_sort	structural basis of allosteric and synergistic activation of ampk by furan-2-phosphonic derivative c2 binding
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/750524f5495343399d0ec23522953a11
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Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding

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