Key result
Recent cryo-electron microscopy structures of the BK channel provide a physical basis for the Horrigan-Aldrich allosteric gating model, explaining how voltage and calcium sensors interact to open the pore.
Why the study?
Although structure-function studies revealed fine details of the BK channel gating mechanism, exact molecular details remained unknown until its quaternary structure was solved at 3.5 A resolution using cryo-electron microscopy.
Recent cryo-EM structures of the BK channel provide a physical basis for the allosteric coupling between voltage and calcium sensing described by the Horrigan-Aldrich model.
BK channel atomic structure now solved; extends prior mutagenesis data but leaves clinical translation open.
The big conductance Ca 2+ -dependent K + channel, also known as BK, MaxiK, Slo1, or KCa1.1, is a ligand- and voltage-gated K + channel. Although structure-function studies of the past decades, involving mutagenesis and electrophysiological measurements, revealed fine details of the mechanism of BK channel gating, the exact molecular details remained unknown until the quaternary structure of the protein has been solved at a resolution of 3.5 Å using cryo-electron microscopy. In this short review, we are going to summarize these results and interpret the gating model of the BK channel in the light of the recent structural results.
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Almássy et al. (2018) conducted a review in BK channel structure and function. Recent cryo-electron microscopy structures of the BK channel provide a physical basis for the Horrigan-Aldrich allosteric gating model, explaining how voltage and calcium sensors interact to open the pore.
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