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
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Acceso en línea:https://doaj.org/article/f14c722416964fa8b99c79a63335b872
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Sumario: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.