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Article

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

Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology - 1 Jan 2008

Brown Scott, Sonntag David P, Sanguinetti Michael C

Abstract excerpt

The central cavity of K(+)-selective ion channels is lined by four S6 transmembrane alpha-helices. An Ala residue is located near the midpoint of each S6 and marks the narrowest point of the central cavity. In hERG1 channels, we determined the functional consequences of substituting this conserved Ala (Ala653) with other hydrophobic or charged amino acids. Mutant channels were expressed in Xenopus oocytes and...

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Identifiers

PMID: 19088442
DOI: 10.1159/000185544
PMCID: PMC2845962

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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.

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

A highly conserved alanine in the S6 domain of the hERG1 K+ channel is required for normal gating.PMID 19088442Read ↗

The evolutionarily conserved residue A653 plays a key role in HERG channel closing.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 ↗

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

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

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

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

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

Role of hydrophobic residues in the voltage sensors of the voltage-gated sodium channel.Semantic proximity Read ↗

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

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

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

NS1643 interacts around L529 of hERG to alter voltage sensor movement on the path to activation.Semantic proximity Read ↗

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