Eukaryotic Kv channel Shaker inactivates through selectivity filter dilation rather than collapse.

ABSTRACT: Eukaryotic voltage-gated K⁺ channels have been extensively studied, but the structural bases for some of their most salient functional features remain to be established. C-type inactivation, for example, is an auto-inhibitory mechanism that confers temporal resolution to their signal-firing activity. In a recent breakthrough, studies of a mutant of Shaker that is prone to inactivate indicated that this process entails a dilation of the selectivity filter, the narrowest part of the ion conduction pathway. Here, we report an atomic-resolution cryo-electron microscopy structure that demonstrates that the wild-type channel can also adopt this dilated state. All-atom simulations corroborate this conformation is congruent with the electrophysiological characteristics of the C-type ina

SUBMITTER: Stix R 

PROVIDER: S-EPMC10708196 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature