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Proc Natl Acad Sci U S A
2012 Aug 21;10934:13579-83. doi: 10.1073/pnas.1207606109.
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Structural insights into neuronal K+ channel-calmodulin complexes.
Mruk K
,
Shandilya SM
,
Blaustein RO
,
Schiffer CA
,
Kobertz WR
.
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Calmodulin (CaM) is a ubiquitous intracellular calcium sensor that directly binds to and modulates a wide variety of ion channels. Despite the large repository of high-resolution structures of CaM bound to peptide fragments derived from ion channels, there is no structural information about CaM bound to a fully folded ion channel at the plasma membrane. To determine the location of CaM docked to a functioning KCNQ K(+) channel, we developed an intracellular tethered blocker approach to measure distances between CaM residues and the ion-conducting pathway. Combining these distance restraints with structural bioinformatics, we generated an archetypal quaternary structural model of an ion channel-CaM complex in the open state. These models place CaM close to the cytoplasmic gate, where it is well positioned to modulate channel function.
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