Systematic Comparison of Molecular Conformations of H+,K+-ATPase Reveals an Important Contribution of the A-M2 Linker for the Luminal Gating

Gastric H+,K+-ATPase, an ATP-driven proton pump responsible for gastric acidification, is a molecular target for anti-ulcer drugs. Here we show its cryo-electron microscopy (EM) structure in an E2P analog state, bound to magnesium fluoride (MgF), and its K+-competitive antagonist SCH28080, determine...

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Veröffentlicht in:	The Journal of biological chemistry 2014-10, Vol.289 (44), p.30590-30601
Hauptverfasser:	Abe, Kazuhiro, Tani, Kazutoshi, Fujiyoshi, Yoshinori
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Anti-Ulcer Agents - chemistry Catalytic Domain Cryoelectron Microscopy H(+)-K(+)-Exchanging ATPase - chemistry H(+)-K(+)-Exchanging ATPase - physiology Imidazoles - chemistry Ion Channel Gating Membrane Biology Models, Molecular Protein Binding Protein Structure, Secondary Proton Pump Inhibitors - chemistry Sus scrofa
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