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Article

Tail end of the s6 segment: role in permeation in shaker potassium channels.

The Journal of general physiology - 1 Jul 2002

Ding Shinghua, Horn Richard

Abstract excerpt

The permeation pathway in voltage-gated potassium channels has narrow constrictions at both the extracellular and intracellular ends. These constrictions might limit the flux of cations from one side of the membrane to the other. The extracellular constriction is the selectivity filter, whereas the intracellular bundle crossing is proposed to act as the activation gate that opens in response to a depolarization....

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 12084778
DOI: 10.1085/jgp.20028611
PMCID: PMC2311402

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tail end of the s6 segment: role in permeation in shaker potassium channels.PMID 12084778Read ↗

Mutations in the S6 gate isolate a late step in the activation pathway and reduce 4-AP sensitivity in shaker K(v) channel.Semantic proximity Read ↗

Gating of shaker-type channels requires the flexibility of S6 caused by prolines.Semantic proximity Read ↗

Hydrophobic substitution mutations in the S4 sequence alter voltage-dependent gating in Shaker K+ channels.Semantic proximity Read ↗

Initial steps in the opening of a Shaker potassium channel.Semantic proximity Read ↗

Investigating the putative glycine hinge in Shaker potassium channel.Semantic proximity Read ↗

S4 mutations alter the single-channel gating kinetics of Shaker K+ channels.Semantic proximity Read ↗

Intracellular gate opening in Shaker K+ channels defined by high-affinity metal bridges.Semantic proximity Read ↗

Role of hydrophobic and ionic forces in the movement of S4 of the Shaker potassium channel.Semantic proximity Read ↗

Hydrophobic interactions between the S5 segment and the pore helix stabilizes the closed state of Slo2.1 potassium channels.Semantic proximity Read ↗

Cross talk between activation and slow inactivation gates of Shaker potassium channels.Semantic proximity Read ↗

The conserved phenylalanine in the K+ channel voltage-sensor domain creates a barrier with unidirectional effects.Semantic proximity Read ↗

Determinants of voltage-dependent gating and open-state stability in the S5 segment of Shaker potassium channels.Semantic proximity Read ↗

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