A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity
2021
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
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.
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