Conformational rearrangement of gastric H+,K+-ATPase induced by an acid suppressant

Kazuhiro Abe, Kazutoshi Tani and Yoshinori Fujiyoshi ()
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Kazuhiro Abe: Faculty of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku
Kazutoshi Tani: Faculty of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku
Yoshinori Fujiyoshi: Faculty of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku

Nature Communications, 2011, vol. 2, issue 1, 1-7

Abstract: Abstract Acid-related gastric diseases are associated with disorder of digestive tract acidification. The gastric proton pump, H+,K+-ATPase, exports H+ in exchange for luminal K+ to generate a highly acidic environment in the stomach, and is a main target for acid suppressants. Here, we report the three-dimensional structure of gastric H+,K+-ATPase with bound SCH28080, a representative K+-competitive acid blocker, at 7 Å resolution based on electron crystallography of two-dimensional crystals. The density of the bound SCH28080 is found near transmembrane (TM) helices 4, 5 and 6, in the luminal cavity. The SCH28080-binding site is formed by the rearrangement of TM helices, which is in turn transmitted to the cytoplasmic domains, resulting in a luminal-open conformation. These results represent the first structural evidence for a binding site of an acid suppressant on H+,K+-ATPase, and the conformational change induced by this class of drugs.

Date: 2011
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DOI: 10.1038/ncomms1154

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