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Article

Structural basis of slow activation gating in the cardiac I Ks channel complex.

Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology - 1 Jan 2011

Strutz-Seebohm Nathalie, Pusch Michael, Wolf Steffen, Stoll Raphael, Tapken Daniel, Gerwert Klaus, Attali Bernard, Seebohm Guiscard

Abstract excerpt

Accessory β-subunits of the KCNE gene family modulate the function of various cation channel α-subunits by the formation of heteromultimers. Among the most dramatic changes of biophysical properties of a voltage-gated channel by KCNEs are the effects of KCNE1 on KCNQ1 channels. KCNQ1 and KCNE1 are believed to form nativeI(Ks) channels. Here, we characterize molecular determinants of KCNE1 interaction with KCNQ1...

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Source

Identifiers

PMID: 21691061
DOI: 10.1159/000329965

Genes

KCNQ1

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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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Structural basis of slow activation gating in the cardiac I Ks channel complex.PMID 21691061Read ↗

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The S4-S5 linker of KCNQ1 channels forms a structural scaffold with the S6 segment controlling gate closure.Semantic proximity Read ↗

Secondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gatingSemantic proximity Read ↗

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