A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity

Romero et al. perform NMR-based screening of 1500 fragments to identify fragments that bind at the oligomeric interface of malate dehydrogenase (MDH). Their study indicates an allosteric mechanism impacting enzymatic activity, paving the way for development of more selective molecules and a starting...

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Autores principales:	Atilio Reyes Romero, Serjey Lunev, Grzegorz M. Popowicz, Vito Calderone, Matteo Gentili, Michael Sattler, Jacek Plewka, Michał Taube, Maciej Kozak, Tad A. Holak, Alexander S. S. Dömling, Matthew R. Groves
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/f14c722416964fa8b99c79a63335b872
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spelling	oai:doaj.org-article:f14c722416964fa8b99c79a63335b8722021-12-02T15:07:46ZA fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity10.1038/s42003-021-02442-12399-3642https://doaj.org/article/f14c722416964fa8b99c79a63335b8722021-08-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02442-1https://doaj.org/toc/2399-3642Romero et al. perform NMR-based screening of 1500 fragments to identify fragments that bind at the oligomeric interface of malate dehydrogenase (MDH). Their study indicates an allosteric mechanism impacting enzymatic activity, paving the way for development of more selective molecules and a starting point for the future development of specific MDH inhibitors.Atilio Reyes RomeroSerjey LunevGrzegorz M. PopowiczVito CalderoneMatteo GentiliMichael SattlerJacek PlewkaMichał TaubeMaciej KozakTad A. HolakAlexander S. S. DömlingMatthew R. GrovesNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Atilio Reyes Romero Serjey Lunev Grzegorz M. Popowicz Vito Calderone Matteo Gentili Michael Sattler Jacek Plewka Michał Taube Maciej Kozak Tad A. Holak Alexander S. S. Dömling Matthew R. Groves A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity
description	Romero et al. perform NMR-based screening of 1500 fragments to identify fragments that bind at the oligomeric interface of malate dehydrogenase (MDH). Their study indicates an allosteric mechanism impacting enzymatic activity, paving the way for development of more selective molecules and a starting point for the future development of specific MDH inhibitors.
format	article
author	Atilio Reyes Romero Serjey Lunev Grzegorz M. Popowicz Vito Calderone Matteo Gentili Michael Sattler Jacek Plewka Michał Taube Maciej Kozak Tad A. Holak Alexander S. S. Dömling Matthew R. Groves
author_facet	Atilio Reyes Romero Serjey Lunev Grzegorz M. Popowicz Vito Calderone Matteo Gentili Michael Sattler Jacek Plewka Michał Taube Maciej Kozak Tad A. Holak Alexander S. S. Dömling Matthew R. Groves
author_sort	Atilio Reyes Romero
title	A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity
title_short	A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity
title_full	A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity
title_fullStr	A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity
title_full_unstemmed	A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity
title_sort	fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f14c722416964fa8b99c79a63335b872
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A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity

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