ArticleNature structural & molecular biology2009
Physical determinants of strong voltage sensitivity of K(+) channel block.
Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026Review
- Inwardly rectifying potassium channels regulate membrane potential polarization and direction sensing during neutrophil chemotaxis.bioRxiv : the preprint server for biology · 2025Article
- Review
- Blockade of TRPV channels by intracellular spermine.The Journal of general physiology · 2023Article
- Kir Channel Molecular Physiology, Pharmacology, and Therapeutic Implications.Handbook of experimental pharmacology · 2021Review
- Polyamine blockade and binding energetics in the MthK potassium channel.The Journal of general physiology · 2020Article
- Atomistic basis of opening and conduction in mammalian inward rectifier potassium (Kir2.2) channels.The Journal of general physiology · 2020Article
- Computational Insights Into Voltage Dependence of Polyamine Block in a Strong Inwardly Rectifying KFrontiers in pharmacology · 2020Article
- Polyamines and potassium channels: A 25-year romance.The Journal of biological chemistry · 2018Review
- Article
- External KThe Journal of general physiology · 2018Article
- Functional mapping of the N-terminal arginine cluster and C-terminal acidic residues of Kir6.2 channel fused to a G protein-coupled receptor.Biochimica et biophysica acta. Biomembranes · 2017Article
- Structure of potassium channels.Cellular and molecular life sciences : CMLS · 2015Review
- Initial steps of inactivation at the K+ channel selectivity filter.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The bundle crossing region is responsible for the inwardly rectifying internal spermine block of the Kir2.1 channel.Pflugers Archiv : European journal of physiology · 2014Article
- Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.The Journal of biological chemistry · 2014Article
- Inward rectifiers and their regulation by endogenous polyamines.Frontiers in physiology · 2014Review
- Scanning the topography of polyamine blocker binding in an inwardly rectifying potassium channel.The Journal of biological chemistry · 2013Article
- Crystal structure of a Ba(2+)-bound gating ring reveals elementary steps in RCK domain activation.Structure (London, England : 1993) · 2012Article
- Interactions of external K+ and internal blockers in a weak inward-rectifier K+ channel.The Journal of general physiology · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Strong voltage sensitivity of inward-rectifier K(+) (Kir) channels has been hypothesized to arise primarily from an intracellular blocker displacing up to five K(+) ions from the wide, intracellular part of the ion conduction pore outwardly across the narrow ion-selectivity filter. The validity of this hypothesis depends on two assumptions: (i) that five ion sites are located intracellular to the filter and (ii) that the blocker can force essentially unidirectional K(+) movement in a pore region generally wider than the combined dimensions of the blocker plus a K(+) ion. Here we present a crystal structure of the cytoplasmic portion of a Kir channel with five ions bound and demonstrate that a constriction near the intracellular end of the pore, acting as a gasket, prevents K(+) ions from bypassing the blocker. This heretofore unrecognized 'gasket' ensures that the blocker can effectively displace K(+) ions across the selectivity filter to generate exceedingly strong voltage sensitivity.
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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.