Molecular structures of the human Slo1 K⁺ channel in complex with β4.

ABSTRACT: Slo1 is a Ca²⁺- and voltage-activated K⁺ channel that underlies skeletal and smooth muscle contraction, audition, hormone secretion and neurotransmitter release. In mammals, Slo1 is regulated by auxiliary proteins that confer tissue-specific gating and pharmacological properties. This study presents cryo-EM structures of Slo1 in complex with the auxiliary protein, β4. Four β4, each containing two transmembrane helices, encircle Slo1, contacting it through helical interactions inside the membrane. On the extracellular side, β4 forms a tetrameric crown over the pore. Structures with high and low Ca²⁺ concentrations show that identical gating conformations occur in the absence and presence of β4, implying that β4 serves to modulate the relative stabilities of

SUBMITTER: Tao X 

PROVIDER: S-EPMC6934384 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature