Key result
The extracellular ends of β1 TM2 and α S0 are in contact, and β1 TM1 is close to both S1 and S2, with cross-linking generally shifting conductance-voltage curves toward more positive potentials.
Population
BK potassium channels (alpha and beta1 subunits)
Design
Preclinical
Authors
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Structural mapping of BK subunits in animals extends mechanistic models; leaves open human translation.
The study maps the structural interactions between the beta1 and alpha subunits of the BK potassium channel, providing mechanistic insights into its modulation.
Liu et al. (2008) studied this question. Cysteine substitution and disulfide cross-linking vs. Wild-type or pseudo-wild-type channels was evaluated on Extent of endogenous disulfide bond formation and functional effects on channel gating. The extracellular ends of β1 TM2 and α S0 are in contact, and β1 TM1 is close to both S1 and S2, with cross-linking generally shifting conductance-voltage curves toward more positive potentials.
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