ArticleNature structural & molecular biology2007
Conformational dynamics of the KcsA potassium channel governs gating properties.
Article in Nature structural & molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.
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Who cites it
65 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Ion Selectivity in the ENaC/DEG Family: A Systematic Review with Supporting Analysis.International journal of molecular sciences · 2021Pooled it
- Gating crosstalk in potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Article
- Central cavity dehydration as a gating mechanism of potassium channels.Nature communications · 2023Article
- High-Resolution Magic Angle Spinning NMR of KcsA in Liposomes: The Highly Mobile C-Terminus.Biomolecules · 2022Article
- Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR.Membranes · 2021Review
- Molecular Mechanisms for Bacterial Potassium Homeostasis.Journal of molecular biology · 2021Review
- Unraveling of a Strongly Correlated Dynamical Network of Residues Controlling the Permeation of Potassium in KcsA Ion Channel.Entropy (Basel, Switzerland) · 2021Article
- Tetraoctylammonium, a Long Chain Quaternary Ammonium Blocker, Promotes a Noncollapsed, Resting-Like Inactivated State in KcsA.International journal of molecular sciences · 2021Article
- Conformational equilibrium shift underlies altered KNature communications · 2020Article
- Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020Review
- Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR.International journal of molecular sciences · 2020Review
- Optimal transport and colossal ionic mechano-conductance in graphene crown ethers.Science advances · 2019Article
- Accessibility of Cations to the Selectivity Filter of KcsA in the Inactivated State: An Equilibrium Binding Study.International journal of molecular sciences · 2019Article
- Shifts in the selectivity filter dynamics cause modal gating in KNature communications · 2019Article
- Rapid constriction of the selectivity filter underlies C-type inactivation in the KcsA potassium channel.The Journal of general physiology · 2018Article
- Site-specific ion occupation in the selectivity filter causes voltage-dependent gating in a viral KScientific reports · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Selective exclusion and selective binding both contribute to ion selectivity in KcsA, a model potassium channel.The Journal of biological chemistry · 2017Article
5 more citing papers are in PubMed but not listed here.
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5 authors.
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Abstract
K+ channels conduct and regulate K+ flux across the cell membrane. Several crystal structures and biophysical studies of tetrameric ion channels have revealed many of the structural details of ion selectivity and gating. A narrow pore lined with four arrays of carbonyl groups is responsible for ion selectivity, whereas a conformational change of the four inner transmembrane helices (TM2) is involved in gating. We used NMR to examine full-length KcsA, a prototypical K+ channel, in its open, closed and intermediate states. These studies reveal that at least two conformational states exist both in the selectivity filter and near the C-terminal ends of the TM2 helices. In the ion-conducting open state, we observed rapid structural exchange between two conformations of the filter, presumably of low and high K+ affinity, respectively. Such measurements of millisecond-timescale dynamics reveal the basis for simultaneous ion selection and gating.
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