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Article

Role of transmembrane segment S5 on gating of voltage-dependent K+ channels.

The Journal of general physiology - 1 Jun 1997

Shieh C C, Klemic K G, Kirsch G E

Abstract excerpt

The cytoplasmic half of S5 (5'S5) has been identified as part of the inner mouth of the pore based on evidence that mutations in this region greatly alter single channel conductance, 4-aminopyridine (4-AP) block and the rate of channel closing upon repolarization (deactivation). The latter effect...

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Identifiers

PMID: 9222902
DOI: 10.1085/jgp.109.6.767
PMCID: PMC2217039

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-9222902-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Role of transmembrane segment S5 on gating of voltage-dependent K+ channels.PMID 9222902Read ↗

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The S4-S5 linker acts as a signal integrator for HERG K+ channel activation and deactivation gating.Semantic proximity Read ↗

KCNQ1 channels voltage dependence through a voltage-dependent binding of the S4-S5 linker to the pore domain.Semantic proximity Read ↗

Voltage-insensitive gating after charge-neutralizing mutations in the S4 segment of Shaker channels.Semantic proximity Read ↗

Dual role of the S5 segment in type 1 ryanodine receptor channel gating.Semantic proximity Read ↗

Mutations within the S4-S5 linker alter voltage sensor constraints in hERG K+ channels.Semantic proximity Read ↗

KCNE1 remodels the voltage sensor of Kv7.1 to modulate channel function.Semantic proximity Read ↗

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

A highly conserved alanine in the S6 domain of the hERG1 K+ channel is required for normal gating.Semantic proximity Read ↗

Hydrophobic interactions between the voltage sensor and pore mediate inactivation in Kv11.1 channels.Semantic proximity Read ↗

Distinct roles of the last transmembrane domain in controlling Arabidopsis K+ channel activity.Semantic proximity Read ↗

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