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Article

Tryptophan scanning mutagenesis of the HERG K+ channel: the S4 domain is loosely packed and likely to be lipid exposed.

The Journal of physiology - 1 Dec 2005

Subbiah Rajesh N, Kondo Mari, Campbell Terence J, Vandenberg Jamie I

Abstract excerpt

Inherited mutations or drug-induced block of voltage-gated ion channels, including the human ether-à-go-go-related gene (HERG) K+ channel, are significant causes of malignant arrhythmias and sudden death. The fourth transmembrane domain (S4) of these channels contains multiple positive charges th...

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Identifiers

PMID: 16166152
DOI: 10.1113/jphysiol.2005.097386
PMCID: PMC1464230

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16166152-2026-09-02.2. 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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Tryptophan scanning mutagenesis of the HERG K+ channel: the S4 domain is loosely packed and likely to be lipid exposed.PMID 16166152Read ↗

The neutral, hydrophobic isoleucine at position I521 in the extracellular S4 domain of hERG contributes to channel gating equilibrium.Semantic proximity Read ↗

Molecular basis of slow activation of the human ether-a-go-go related gene potassium channel.Semantic proximity Read ↗

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

Voltage sensor movement in the hERG K+ channel.Semantic proximity Read ↗

Allosteric effects of mutations in the extracellular S5-P loop on the gating and ion permeation properties of the hERG potassium channel.Semantic proximity Read ↗

The hERG K(+) channel S4 domain L532P mutation: characterization at 37°C.Semantic proximity Read ↗

A novel missense mutation causing a G487R substitution in the S2-S3 loop of human ether-à-go-go-related gene channel.Semantic proximity Read ↗

Functional interactions of voltage sensor charges with an S2 hydrophobic plug in hERG channels.Semantic proximity Read ↗

The Fast Component of hERG Gating Charge: An Interaction between D411 in the S1 and S4 Residues.Semantic proximity Read ↗

Cooperative interactions between R531 and acidic residues in the voltage sensing module of hERG1 channels.Semantic proximity Read ↗

Fast and slow voltage sensor movements in HERG potassium channels.Semantic proximity Read ↗

Blockade of permeation by potassium but normal gating of the G628S nonconducting hERG channel mutant.Semantic proximity Read ↗

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