The Topology of the α, β Subunits of the Gastric H/K ATPase

  • Jai Moo Shin
  • Krister Bamberg
  • Marie Besancon
  • Keith Munson
  • Frederic Mercier
  • Dennis Bayle
  • Steve Hersey
  • George Sachs
Conference paper
Part of the NATO ASI Series book series (NATO ASI, volume 89)


Knowledge of the secondary structure of the gastric H/K ATPase,a P type transport ATPase, allows deductions as to the ion transport pathway across the membrane spanning domain of the large, 1033 amino acid catalytic a subunit and as to the site of interaction between the smaller, glycosylated, ß subunit and the or subunit. The structure of this region of the enzyme also allows us to understand the molecular basis for inhibition of acid secretion by acid pump inhibitors, such as the substituted benzimidazoles and the K+ competitive type of H/K ATPase inhibitor.


Membrane Anchor Membrane Span Domain Membrane Span Membrane Segment Hydropathy Plot 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer-Verlag Berlin Heidelberg 1994

Authors and Affiliations

  • Jai Moo Shin
    • 1
  • Krister Bamberg
    • 1
  • Marie Besancon
    • 1
  • Keith Munson
    • 1
  • Frederic Mercier
    • 1
  • Dennis Bayle
    • 1
  • Steve Hersey
    • 2
  • George Sachs
    • 1
  1. 1.UCLA and Wadsworth VAMCLos AngelesUSA
  2. 2.Emory UniversityAtlantaUSA

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