Abstract
Ligand binding sites within ion channel domains can interact by allosteric mechanisms, to modulate binding and control channel function. By determining crystal structures of regulator of K conductance (RCK) domains from K+ channels, we identify possible mechanisms of allosteric coupling among Ca2+ regulatory sites in the channel. Combining this structural analysis with complementary electrophysiological analysis of channel gating, we arrive at a working hypothesis for chemical interactions that are important for modulation of ligand binding and subsequent channel opening.
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