Molecular interactions of the Na<sub>V</sub>1.5 C-terminal domain: CaM sequestered the IQ motif from the CTD.
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ABSTRACT: Voltage-gated sodium channels (NaV) are important for life. Alterations to the synchronized timing of ion conduction can create life-threatening conditions. How NaV conduction responds to changes in intracellular Ca2+ concentration has been the subject of extensive investigation. Crystal structures of the cardiac NaV (NaV1.5) cytosolic components were reported as trimeric complexes that are restructured in the presence of Ca2+. These results formed the basis for a gating model where two NaV1.5 molecules interact to alter function in response to Ca2+ concentration. Here, we investigated the binding site surface of these trimeric interactions in solution. Nuclear magnetic resonance spectroscopy demonstrat
SUBMITTER: Gyawu RF
PROVIDER: S-EPMC12682251 | biostudies-literature | 2025 Oct
REPOSITORIES: biostudies-literature
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