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The \u03b1 subunit with molecular mass of about 100 kDa has 10 transmembrane domains and is strongly associated with the \u03b2 subunit with a single transmembrane segment and a peptide mass of 35 kDa. Its three\u2010dimensional structure is based on homology modeling and site\u2010directed mutagenesis resulting in a proton extrusion and K<jats:sup>+<\/jats:sup>reabsorption model. There are three conserved H<jats:sub>3<\/jats:sub>O<jats:sup>+<\/jats:sup>\u2010binding sites in the middle of the membrane domain and H<jats:sub>3<\/jats:sub>O<jats:sup>+<\/jats:sup>secretion depends on a conformational change involving Lys<jats:sup>791<\/jats:sup>insertion into the second H<jats:sub>3<\/jats:sub>O<jats:sup>+<\/jats:sup>site enclosed by E795, E820, and D824 that allows export of protons at a concentration of 160 mM. K<jats:sup>+<\/jats:sup>countertransport involves binding to this site after the release of protons with retrograde displacement of Lys<jats:sup>791<\/jats:sup>and then K<jats:sup>+<\/jats:sup>transfer to E343 and exit to the cytoplasm. This ATPase is the major therapeutic target in treatment of acid\u2010related diseases and there are several known luminal inhibitors allowing analysis of the luminal vestibule. One class contains the acid\u2010activated covalent, thiophilic proton pump inhibitors, the most effective of current acid\u2010suppressive drugs. Their binding sites and trypsinolysis allowed identification of all ten transmembrane segments of the ATPase. In addition, various K<jats:sup>+<\/jats:sup>\u2010competitive inhibitors of the ATPase are being developed, with the advantage of complete and rapid inhibition of acid secretion independent of pump activity and allowing further refinement of the structure of the luminal vestibule of the E<jats:sub>2<\/jats:sub>form of this ATPase. \u00a9 2011 American Physiological Society.<jats:italic>Compr Physiol<\/jats:italic>1:2141\u20102153, 2011.<\/jats:p>","DOI":"10.1002\/cphy.c110010","type":"other","created":{"date-parts":[[2011,9,19]],"date-time":"2011-09-19T16:33:29Z","timestamp":1316450009000},"page":"2141-2153","source":"Crossref","is-referenced-by-count":16,"title":["Gastric H<sup>+<\/sup>,K<sup>+<\/sup>\u2010<scp>ATP<\/scp>ase"],"prefix":"10.1002","author":[{"given":"Jai Moo","family":"Shin","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Keith","family":"Munson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"George","family":"Sachs","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2011,10]]},"reference":[{"key":"e_1_2_7_2_1_1","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms1154"},{"key":"e_1_2_7_2_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/emboj.2009.102"},{"key":"e_1_2_7_2_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.275.12.8324"},{"key":"e_1_2_7_2_4_1","doi-asserted-by":"crossref","first-page":"22167","DOI":"10.1016\/S0021-9258(18)45685-2","article-title":"Reversible inhibitions of gastric H+,K(+)\u2010ATPase by scopadulcic acid B and diacetyl scopadol. 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