ArticleJournal of molecular biology2010
Conformational dynamics in the selectivity filter of KcsA in response to potassium ion concentration.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- Ligand Binding Dynamics of Ion Channels and GPCRs Using Single-Molecule Fluorescence.Annual review of biophysics · 2026Review
- Very broad distribution of β sheet registries of the HIV gp41 fusion peptide supports mutational robustness for fusion and infection.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Water inside the Selectivity Filter of a KJournal of the American Chemical Society · 2024Article
- Article
- High-Resolution Magic Angle Spinning NMR of KcsA in Liposomes: The Highly Mobile C-Terminus.Biomolecules · 2022Article
- Pore-forming transmembrane domains control ion selectivity and selectivity filter conformation in the KirBac1.1 potassium channel.The Journal of general physiology · 2021Article
- Informing NMR experiments with molecular dynamics simulations to characterize the dominant activated state of the KcsA ion channel.The Journal of chemical physics · 2021Article
- NMR studies of lipid regulation of the KBiochimica et biophysica acta. Biomembranes · 2021Article
- Tetraoctylammonium, a Long Chain Quaternary Ammonium Blocker, Promotes a Noncollapsed, Resting-Like Inactivated State in KcsA.International journal of molecular sciences · 2021Article
- Structural Plasticity of the Selectivity Filter in Cation Channels.Frontiers in physiology · 2021Review
- Selectivity filter ion binding affinity determines inactivation in a potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conformational equilibrium shift underlies altered KNature communications · 2020Article
- Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020Review
- Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structures Illuminate Cardiac Ion Channel Functions in Health and in Long QT Syndrome.Frontiers in pharmacology · 2020Review
- Equilibria between the KProtein & cell · 2019Article
- The conduction pathway of potassium channels is water free under physiological conditions.Science advances · 2019Article
- Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies.Scientific reports · 2019Article
- Potassium channel selectivity filter dynamics revealed by single-molecule FRET.Nature chemical biology · 2019Article
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4 authors.
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Abstract
Conformational change in the selectivity filter of KcsA as a function of ambient potassium concentration is studied with solid-state NMR. This highly conserved region of the protein is known to chelate potassium ions selectively. We report solid-state NMR chemical shift fingerprints of two distinct conformations of the selectivity filter; significant changes are observed in the chemical shifts of key residues in the filter as the potassium ion concentration is changed from 50 mM to 1 muM. Potassium ion titration studies reveal that the site-specific K(d) for K(+) binding at the key pore residue Val76 is on the order of approximately 7 muM and that a relatively high sample hydration is necessary to observe the low-K(+) conformer. Simultaneous detection of both conformers at low ambient potassium concentration suggests that the high-K(+) and low-K(+) states are in slow exchange on the NMR timescale (k(ex)<500 s(-)(1)). The slow rate and tight binding for evacuating both inner sites simultaneously differ from prior observations in detergent in solution, but agree well with measurements by electrophysiology and appear to result from our use of a hydrated bilayer environment. These observations strongly support a common assumption that the low-K(+) state is not involved in ion transmission, and that during transmission one of the two inner sites is always occupied. On the other hand, these kinetic and thermodynamic characteristics of the evacuation of the inner sites certainly could be compatible with participation in a control mechanism at low ion concentration such as C-type inactivation, a process that is coupled to activation and involves closing of the outer mouth of the channel.
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