The study reveals that the gating ring of BK channels is a flexible structure capable of complex, independent conformational changes triggered by different divalent ions.
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Enhances molecular models of BK channel gating; leaves open selective modulation for vascular disease.
Significance Large-conductance voltage- and calcium-activated K + (BK) channels are allosterically regulated by intracellular Ca 2+ and voltage. The Ca 2+ sensor is a large tetrameric structure called the “gating ring.” Each subunit of this structure contains two distinct regulator of conductance of potassium (RCK) domains, each contributing one Ca 2+ binding site. Both sites have a different selectivity for Ca 2+ , Mg 2+ , Cd 2+ , and Ba 2+ . Using FRET, we monitored the conformational changes of different regions of the gating ring upon binding of divalent ions. Our results reveal the existence of additive and independent motions by the two RCK domains that form the gating ring. These results indicate that the gating ring is a flexible structure capable of complex conformational changes that can be triggered specifically by different divalent ions.
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Miranda et al. (2016) studied this question.
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