Molecular dissection of multiphase inactivation of the bacterial sodium channel Na_VAb.

ABSTRACT: Homotetrameric bacterial voltage-gated sodium channels share major biophysical features with their more complex eukaryotic counterparts, including a slow-inactivation mechanism that reduces ion-conductance activity during prolonged depolarization through conformational changes in the pore. The bacterial sodium channel Na_VAb activates at very negative membrane potentials and inactivates through a multiphase slow-inactivation mechanism. Early voltage-dependent inactivation during one depolarization is followed by late use-dependent inactivation during repetitive depolarization. Mutations that change the molecular volume of Thr206 in the pore-lining S6 segment can enhance or strongly block early voltage-dependent inactivation, suggesting that this residue serves as a molecular hub

SUBMITTER: Gamal El-Din TM 

PROVIDER: S-EPMC6363407 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature