Key result
Disulfide crosslinking maps BK beta4 TM2 near alpha S0 and TM1 near alpha S1 and S2.
Population
BK potassium channels composed of alpha and beta 4 subunits
Design
Preclinical
Authors
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Defines beta4-alpha TM interfaces in BK channels; leaves open functional consequences pending validation in native systems.
The study maps the structural proximity of beta 4 transmembrane helices to alpha helices in BK potassium channels, demonstrating that TM2 is close to S0 and TM1 is close to S1 and S2.
Wu et al. (2009) studied this question. Cysteine substitution and disulfide crosslinking was evaluated on Extent of disulfide bond formation between substituted cysteines. Disulfide crosslinking revealed that the BK channel beta4 TM2 helix is close to alpha S0, and beta4 TM1 is close to both alpha S1 and S2.
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