Potential C-terminal domain interactions of the cardiac voltage gated sodium channel.

ABSTRACT: CryoEM structural characterization of the cardiac sodium channel (Na_V1.5) captured the cytosolic C-terminal domain (CTD) interacting with the cytosolic loop that connects domains III and IV (inactivation gate). Our previous modeling efforts focused on improving descriptions of the cytosolic components and unexpectedly captured dissociation of this complex. Other reports have provided evidence of CTD interaction with a different cytosolic Na_V1.5 component. Specifically, NMR spectroscopy demonstrated that a reconstituted CTD (93 amino acids construct, helices I-IV) could engage a peptide corresponding to an IQ motif (helix VI) that is also contained on the C-terminus of the Na_V1.5 channel. Here, we leverage recent MD simulation advancements to expand upon thi

SUBMITTER: Lile SK 

PROVIDER: S-EPMC12019241 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature