Ontology highlight
ABSTRACT:
SUBMITTER: Mruk K
PROVIDER: S-EPMC3427091 | biostudies-literature | 2012 Aug
REPOSITORIES: biostudies-literature
Mruk Karen K Shandilya Shiven M D SM Blaustein Robert O RO Schiffer Celia A CA Kobertz William R WR
Proceedings of the National Academy of Sciences of the United States of America 20120806 34
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 d ...[more]