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

Author

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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)

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.

Suggested Citation

  • Kazuhiro Abe & Kazutoshi Tani & Yoshinori Fujiyoshi, 2011. "Conformational rearrangement of gastric H+,K+-ATPase induced by an acid suppressant," Nature Communications, Nature, vol. 2(1), pages 1-7, September.
  • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1154
    DOI: 10.1038/ncomms1154
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