Key result
KCNQ1 position 145C forms disulfide bonds with KCNE1 40C and 41C in activated and resting states, suggesting KCNE1 engages in molecular motions during IKs gating.
Population
COS-7 cells and oocytes expressing KCNQ1 and KCNE1 channel subunits
Comparison
Cysteine substitution mutations in KCNQ1 and KCNE1 vs Native cysteine channels or alternative mutant…
Design
Preclinical
Authors
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Refines IKs gating models via state-dependent contacts; leaves open arrhythmia mechanism targeting.
Identifies specific state-dependent contact points between KCNQ1 and KCNE1 extracellular domains, providing a structural model for IKs channel gating and arrhythmia mechanisms.
Xu et al. (2008) studied this question. Cysteine substitution in KCNQ1 and KCNE1 was evaluated on Disulfide bond formation and gating behavior. KCNQ1 position 145C forms disulfide bonds with KCNE1 40C and 41C in activated and resting states, suggesting KCNE1 engages in molecular motions during IKs gating.
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