| Literature DB >> 28435145 |
Jaroslava Šeflová1, Petra Čechová2, Michal Biler3, Pavel Hradil4, Martin Kubala5.
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.Entities:
Keywords: Binding sites; Inhibition; Na(+)/K(+)-ATPase; Quinolinones; Sodium pump
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Year: 2017 PMID： 28435145 DOI： 10.1016/j.biochi.2017.04.009
Source DB: PubMed Journal: Biochimie ISSN： 0300-9084 Impact factor: 4.079