Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5508969 | Biochimie | 2017 | 6 Pages |
Abstract
Na+/K+-ATPase (NKA) is an enzyme of crucial importance for all animal cells. We examined the inhibitory effects of halogenated phenylquinolinones on NKA. The 5,6,7,8-tetrafluoro-3-hydroxy-2-phenylquinolin-4(1H)-one (TFHPQ) was identified as an efficient NKA inhibitor with IC50 near 10 μM. The inhibition by TFHPQ is particularly efficient at higher concentrations of K+, where NKA adopts the E2 conformation. The experimental observations are in a good agreement with the outcomes from molecular docking. We identified an energetically favourable TFHPQ binding site for the K+-bound NKA, which is located in the proximity of the cytoplasmic C-terminus.
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Authors
Jaroslava Å eflová, Petra Äechová, Michal Biler, Pavel Hradil, Martin Kubala,