ArticleNature structural & molecular biology2011
Protonation of key acidic residues is critical for the K⁺-selectivity of the Na/K pump.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Benchmark Study for Calculations of pKa Values of Metal Ligands in Proteins.Journal of chemical theory and computation · 2026Article
- Protonation of Key Acidic Residues Reveals Binding Features of PCABs to Gastric H, K-ATPase.The Journal of membrane biology · 2026Article
- Derivatization of Bufadienolides at Carbon-3 of the Steroid Core and Their Consequences for the Interaction with NaInternational journal of molecular sciences · 2025Article
- Multistate Kinetic Model of the Sodium-Potassium ATPase.The journal of physical chemistry. B · 2025Article
- Specific protonation of acidic residues confers KThe Journal of biological chemistry · 2024Article
- Ion channel selectivity through ion-modulated changes of selectivity filter pProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Protein pJournal of chemical theory and computation · 2022Article
- Prediction of protein pChemical science · 2022Article
- Allosteric gate modulation confers KThe EMBO journal · 2019Article
- A single KeLife · 2019Article
- Cholesterol depletion inhibits NaThe Journal of biological chemistry · 2019Article
- Distinct pH dependencies of NaThe Journal of biological chemistry · 2018Article
- The CAPOS mutation in ATP1A3 alters Na/K-ATPase function and results in auditory neuropathy which has implications for management.Human genetics · 2018Article
- Molecular simulations and free-energy calculations suggest conformation-dependent anion binding to a cytoplasmic site as a mechanism for NaThe Journal of biological chemistry · 2017Article
- Ion channels and ion selectivity.Essays in biochemistry · 2017Review
- Glutamate Water Gates in the Ion Binding Pocket of NaScientific reports · 2017Article
- Article
- Mechanism of potassium ion uptake by the Na(+)/K(+)-ATPase.Nature communications · 2015Article
- Atomic-level mechanisms for phospholamban regulation of the calcium pump.Biophysical journal · 2015Article
- K+ congeners that do not compromise Na+ activation of the Na+,K+-ATPase: hydration of the ion binding cavity likely controls ion selectivity.The Journal of biological chemistry · 2015Article
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4 authors.
Funding
Abstract
The sodium-potassium (Na/K) pump is a P-type ATPase that generates Na(+) and K(+) concentration gradients across the cell membrane. For each hydrolyzed ATP molecule, the pump extrudes three Na(+) and imports two K(+) by alternating between outward- and inward-facing conformations that preferentially bind K(+) or Na(+), respectively. Remarkably, the selective K(+) and Na(+) binding sites share several residues, and how the pump is able to achieve the selectivity required for the functional cycle is unclear. Here, free energy-perturbation molecular dynamics (FEP/MD) simulations based on the crystal structures of the Na/K pump in a K(+)-loaded state (E2·P(i)) reveal that protonation of the high-field acidic side chains involved in the binding sites is crucial to achieving the proper K(+) selectivity. This prediction is tested with electrophysiological experiments showing that the selectivity of the E2P state for K(+) over Na(+) is affected by extracellular pH.
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