Voltage-dependent activation in EAG channels follows a ligand-receptor rather than a mechanical-lever mechanism.

ABSTRACT: Ether-a-go-go family (EAG) channels play a major role in many physiological processes in humans, including cardiac repolarization and cell proliferation. Cryo-EM structures of two of them, K_V10.1 and human ether-a-go-go-related gene (hERG or K_V11.1), have revealed an original nondomain-swapped structure, suggesting that the mechanism of voltage-dependent gating of these two channels is quite different from the classical mechanical-lever model. Molecular aspects of hERG voltage-gating have been extensively studied, indicating that the S4-S5 linker (S4-S5_L) acts as a ligand binding to the S6 gate (S6 C-terminal part, S6_T) and stabilizes it in a closed state. Moreover, the N-terminal extremity of the channel, called N-Cap, has been suggested to inte

SUBMITTER: Malak OA 

PROVIDER: S-EPMC6484144 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature