Abstract
Among ion channels, the large-conductance Ca2+-activated K+ channel (BKCa channel) is in many ways unique. It has a very large single-channel conductance—ten times that of most vertebrate K+ channels—and yet it maintains strict K+ selectivity. It senses as little as 200 nM Ca2+, but it contains no consensus Ca2+-binding motifs, and it is the only channel to be activated by both intracellular Ca2+ and membrane voltage. In fact, there is a synergy between these stimuli such that the higher the internal Ca2+ concentration ([Ca2+]), the smaller the depolarization needed to activate the channel. Furthermore, the BKCa channel has its own brand of auxiliary subunits that profoundly affect gating. In this chapter, I will discuss what is understood about the origins of these properties in terms of allosteric models and channel structure. At the outset, however, I should say that there is not yet a crystal structure of the BKCa channel or any of its components, so much of the current thinking about BKCa-channel structure relies on analogy to other channels.
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Cox, D.H. (2007). BKCa-Channel Structure and Function. In: Chung, SH., Andersen, O.S., Krishnamurthy, V. (eds) Biological Membrane Ion Channels. Biological And Medical Physics Biomedical Engineering. Springer, New York, NY. https://doi.org/10.1007/0-387-68919-2_5
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