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• W2062078340 startingPage "609" @default.
• W2062078340 abstract "The gastric H,K-ATPase, a member of the P(2)-type ATPase family, is the integral membrane protein responsible for gastric acid secretion. It is an alpha,beta-heterodimeric enzyme that exchanges cytoplasmic hydronium with extracellular potassium. The catalytic alpha subunit has ten transmembrane segments with a cluster of intramembranal carboxylic amino acids located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8. Comparison to the known structure of the SERCA pump, mutagenesis, and molecular modeling has identified these as constituents of the ion binding domain. The beta subunit has one transmembrane segment with N terminus in cytoplasmic region. The extracellular domain of the beta subunit contains six or seven N-linked glycosylation sites. N-glycosylation is important for the enzyme assembly, maturation, and sorting. The enzyme pumps acid by a series of conformational changes from an E(1) (ion site in) to an E(2) (ion site out) configuration following binding of MgATP and phosphorylation. Several experimental observations support the hypothesis that expulsion of the proton at 160 mM (pH 0.8) results from movement of lysine 791 into the ion binding site in the E(2)P configuration. Potassium access from the lumen depends on activation of a K and Cl conductance via a KCNQ1/KCNE2 complex and Clic6. K movement through the luminal channel in E(2)P is proposed to displace the lysine along with dephosphorylation to return the enzyme to the E(1) configuration. This enzyme is inhibited by the unique proton pump inhibitor class of drug, allowing therapy of acid-related diseases." @default.
• W2062078340 created "2016-06-24" @default.
• W2062078340 creator A5008732364 @default.
• W2062078340 creator A5019676161 @default.
• W2062078340 creator A5057185561 @default.
• W2062078340 creator A5075537726 @default.
• W2062078340 date "2008-06-06" @default.
• W2062078340 modified "2023-10-10" @default.
• W2062078340 title "The gastric HK-ATPase: structure, function, and inhibition" @default.
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• W2062078340 doi "https://doi.org/10.1007/s00424-008-0495-4" @default.
• W2062078340 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3079481" @default.
• W2062078340 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18536934" @default.
• W2062078340 hasPublicationYear "2008" @default.
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