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Article

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

Biophysical journal - 3 Nov 2010

Van Slyke Aaron C, Rezazadeh Saman, Snopkowski Mischa, Shi Patrick, Allard Charlene R, Claydon Tom W

Abstract excerpt

Human ether-a-go-go related gene (hERG) channel gating is associated with slow activation, yet the mechanistic basis for this is unclear. Here, we examine the effects of mutation of a unique glycine residue (G546) in the S4-S5 linker on voltage sensor movement and its coupling to pore gating. Sub...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 21044581
DOI: 10.1016/j.bpj.2010.08.030
PMCID: PMC2965951

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21044581-2026-09-02.2. 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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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations within the S4-S5 linker alter voltage sensor constraints in hERG K+ channels.PMID 21044581Read ↗

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

Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes.Semantic proximity Read ↗

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

The pore domain outer helix contributes to both activation and inactivation of the HERG K+ channel.Semantic proximity Read ↗

Stabilization of the Activated hERG Channel Voltage Sensor by Depolarization Involves the S4-S5 Linker.Semantic proximity Read ↗

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

Interactions between the N-terminal tail and the gating machinery of hERG K⁺ channels both in closed and open/inactive states.Semantic proximity Read ↗

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

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

Potassium dependent structural changes in the selectivity filter of HERG potassium channelsSemantic proximity Read ↗

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

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