ArticleThe Journal of general physiology2011
Potassium-selective block of barium permeation through single KcsA channels.
Article in The Journal of general physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Barium senses subtle pore changes in a voltage-gated KScience advances · 2026Article
- Mutation in pore-helix modulates interplay between filter gate and Ba2+ block in a Kcv channel pore.The Journal of general physiology · 2024Article
- A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V.Nature communications · 2022Article
- Unraveling of a Strongly Correlated Dynamical Network of Residues Controlling the Permeation of Potassium in KcsA Ion Channel.Entropy (Basel, Switzerland) · 2021Article
- 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
- A Functional KViruses · 2020Article
- Open and Closed Structures of a Barium-Blocked Potassium Channel.Journal of molecular biology · 2020Article
- Identification of a G-Protein-Independent Activator of GIRK Channels.Cell reports · 2020Article
- A small viral potassium ion channel with an inherent inward rectification.Channels (Austin, Tex.) · 2019Article
- Queueing arrival and release mechanism for KThe journal of physiological sciences : JPS · 2019Article
- Reconstitution and functional characterization of ion channels from nanodiscs in lipid bilayers.The Journal of general physiology · 2018Article
- Transmembrane allosteric energetics characterization for strong coupling between proton and potassium ion binding in the KcsA channel.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mechanism of single- and double-sided inhibition of dual topology fluoride channels by synthetic monobodies.The Journal of general physiology · 2017Article
- Hysteresis of KcsA potassium channel's activation- deactivation gating is caused by structural changes at the channel's selectivity filter.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Pore size matters for potassium channel conductance.The Journal of general physiology · 2016Review
- Multi-ion free energy landscapes underscore the microscopic mechanism of ion selectivity in the KcsA channel.Biochimica et biophysica acta · 2016Article
- bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles.The Journal of general physiology · 2016Article
- Designer and natural peptide toxin blockers of the KcsA potassium channel identified by phage display.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Determinants of cation transport selectivity: Equilibrium binding and transport kinetics.The Journal of general physiology · 2015Review
- Two-sided block of a dual-topology F- channel.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Ba(2+), a doubly charged analogue of K(+), specifically blocks K(+) channels by virtue of electrostatic stabilization in the permeation pathway. Ba(2+) block is used here as a tool to determine the equilibrium binding affinity for various monovalent cations at specific sites in the selectivity filter of a noninactivating mutant of KcsA. At high concentrations of external K(+), the block-time distribution is double exponential, marking at least two Ba(2+) sites in the selectivity filter, in accord with a Ba(2+)-containing crystal structure of KcsA. By analyzing block as a function of extracellular K(+), we determined the equilibrium dissociation constant of K(+) and of other monovalent cations at an extracellular site, presumably S1, to arrive at a selectivity sequence for binding at this site: Rb(+) (3 µM) > Cs(+) (23 µM) > K(+) (29 µM) > NH(4)(+) (440 µM) >> Na(+) and Li(+) (>1 M). This represents an unusually high selectivity for K(+) over Na(+), with |ΔΔG(0)| of at least 7 kcal mol(-1). These results fit well with other kinetic measurements of selectivity as well as with the many crystal structures of KcsA in various ionic conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.