Key result
KCNE1 binds to the outer face of the KCNQ1 channel pore domain, modifying interactions between the voltage sensor, S4-S5 linker, and pore domain to induce slow activation gating.
Population
Molecular models and mutants of KCNQ1 and KCNE1 cardiac ion channels
Design
Preclinical
Authors
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Elucidates KCNE1-KCNQ1 interactions in I(Ks) gating; leaves open validation for modeling LQTS mutants.
The study provides a new KCNQ1-KCNE1 structural model that elucidates the basis of slow activation gating in cardiac I(Ks) channels, which may be useful for modeling disease-associated mutants.
Strutz‐Seebohm et al. (2011) studied Cardiac I(Ks) channel complex function. Scanning mutagenesis and molecular dynamics simulations was evaluated on Molecular determinants of KCNE1 interaction with KCNQ1 channels. KCNE1 binds to the outer face of the KCNQ1 channel pore domain, modifying interactions between the voltage sensor, S4-S5 linker, and pore domain to induce slow activation gating.
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