Structural basis of voltage-dependent gating in BK channels.

ABSTRACT: The allosteric communication between the pore domain, voltage sensors, and Ca²⁺ binding sites in the calcium- and voltage-activated K⁺ channel (BK) underlies its physiological role as the preeminent signal integrator in excitable systems. BK displays shallow voltage sensitivity with very fast gating charge kinetics, yet little is known about the molecular underpinnings of this distinctive behavior. Here, we explore the mechanistic basis of coupling between voltage-sensing domains (VSDs) and calcium sensors in Aplysia BK by locking the VSDs in their activated (R196Q and R199Q) and resting (R202Q) states, with or without calcium. Cryo-EM structures of these mutants reveal unique tilts at the S4 C-terminal end, together with large side-chain rotameric excursions of the g

SUBMITTER: Contreras GF 

PROVIDER: S-EPMC12218146 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature