Abstract
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.
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© 1994 Springer-Verlag Berlin Heidelberg
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Shin, J.M. et al. (1994). The Topology of the α, β Subunits of the Gastric H/K ATPase. In: Hirst, B.H. (eds) Molecular and Cellular Mechanisms of H+ Transport. NATO ASI Series, vol 89. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79301-1_5
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DOI: https://doi.org/10.1007/978-3-642-79301-1_5
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