ArticleThe Journal of general physiology2014
Ionic interactions of Ba2+ blockades in the MthK K+ channel.
Article in The Journal of general physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Mutation in pore-helix modulates interplay between filter gate and Ba2+ block in a Kcv channel pore.The Journal of general physiology · 2024Article
- Structural bases for blockade and activation of BK channels by BaFrontiers in molecular biosciences · 2024Article
- A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V.Nature communications · 2022Article
- 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
- Open and Closed Structures of a Barium-Blocked Potassium Channel.Journal of molecular biology · 2020Article
- A small viral potassium ion channel with an inherent inward rectification.Channels (Austin, Tex.) · 2019Article
- Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling.Nature communications · 2019Article
- Calcium channel gating.Pflugers Archiv : European journal of physiology · 2018Review
- Determinants of cation transport selectivity: Equilibrium binding and transport kinetics.The Journal of general physiology · 2015Review
- The conserved potassium channel filter can have distinct ion binding profiles: structural analysis of rubidium, cesium, and barium binding in NaK2K.The Journal of general physiology · 2014Article
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Authors and funding
5 authors.
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Abstract
The movement and interaction of multiple ions passing through in single file underlie various fundamental K(+) channel properties, from the effective conduction of K(+) ions to channel blockade by Ba(2+) ions. In this study, we used single-channel electrophysiology and x-ray crystallography to probe the interactions of Ba(2+) with permeant ions within the ion conduction pathway of the MthK K(+) channel. We found that, as typical of K(+) channels, the MthK channel was blocked by Ba(2+) at the internal side, and the Ba(2+)-blocking effect was enhanced by external K(+). We also obtained crystal structures of the MthK K(+) channel pore in both Ba(2+)-Na(+) and Ba(2+)-K(+) environments. In the Ba(2+)-Na(+) environment, we found that a single Ba(2+) ion remained bound in the selectivity filter, preferably at site 2, whereas in the Ba(2+)-K(+) environment, Ba(2+) ions were predominantly distributed between sites 3 and 4. These ionic configurations are remarkably consistent with the functional studies and identify a molecular basis for Ba(2+) blockade of K(+) channels.
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