A Conformation-specific Interhelical Salt Bridge in the K+ Binding Site of Gastric H,K-ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference45 articles.
1. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
2. Role of Negatively Charged Residues in the Fifth and Sixth Transmembrane Domains of the Catalytic Subunit of Gastric H+,K+-ATPase
3. The negative charge of glutamic acid-820 in the gastric H+,K+-ATPase α-subunit is essential for K+ activation of the enzyme activity
4. Mutational Analysis of the K+-Competitive Inhibitor Site of Gastric H,K-ATPase
5. The Carbonyl Group of Glutamic Acid-795 Is Essential for Gastric H+,K+-ATPase Activity
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1. Na+,K+-ATPase with Disrupted Na+ Binding Sites I and III Binds Na+ with Increased Affinity at Site II and Undergoes Na+-Activated Phosphorylation with ATP;Biomolecules;2024-01-22
2. Specific protonation of acidic residues confers K+ selectivity to the gastric proton pump;Journal of Biological Chemistry;2024-01
3. A single K+-binding site in the crystal structure of the gastric proton pump;eLife;2019-08-22
4. A single K+-binding site in the crystal structure of the gastric proton pump;2019-04-15
5. K+ binding and proton redistribution in the E2P state of the H+, K+-ATPase;Scientific Reports;2018-08-24
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