Ion-pair interactions between voltage-sensing domain IV and pore domain I regulate Ca_V1.1 gating.

ABSTRACT: The voltage-gated calcium channel Ca_V1.1 belongs to the family of pseudo-heterotetrameric cation channels, which are built of four structurally and functionally distinct voltage-sensing domains (VSDs) arranged around a common channel pore. Upon depolarization, positive gating charges in the S4 helices of each VSD are moved across the membrane electric field, thus generating the conformational change that prompts channel opening. This sliding helix mechanism is aided by the transient formation of ion-pair interactions with countercharges located in the S2 and S3 helices within the VSDs. Recently, we identified a domain-specific ion-pair partner of R1 and R2 in VSD IV of Ca_V1.1 that stabilizes the activated state of this VSD and regulates the voltage dependence of curre

SUBMITTER: El Ghaleb Y 

PROVIDER: S-EPMC8553663 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature