Chemometric Models of Differential Amino Acids at the Na_vα and Na_vβ Interface of Mammalian Sodium Channel Isoforms.

ABSTRACT: (1) Background: voltage-gated sodium channels (Na_vs) are integral membrane proteins that allow the sodium ion flux into the excitable cells and initiate the action potential. They comprise an α (Na_vα) subunit that forms the channel pore and are coupled to one or more auxiliary β (Na_vβ) subunits that modulate the gating to a variable extent. (2) Methods: after performing homology in silico modeling for all nine isoforms (Na_v1.1α to Na_v1.9α), the Na_vα and Na_vβ protein-protein interaction (PPI) was analyzed chemometrically based on the primary and secondary structures as well as topological or spatial mapping. (3) Results: our findings reveal a unique isoform-specific correspondence between certain segments of the ex

SUBMITTER: Villa-Diaz F 

PROVIDER: S-EPMC7435598 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature