Architecture and assembly mechanism of native glycine receptors.

ABSTRACT: Glycine receptors (GlyRs) are pentameric, 'Cys-loop' receptors that form chloride-permeable channels and mediate fast inhibitory signalling throughout the central nervous system^1,2. In the spinal cord and brainstem, GlyRs regulate locomotion and cause movement disorders when mutated^2,3. However, the stoichiometry of native GlyRs and the mechanism by which they are assembled remain unclear, despite extensive investigation^4-8. Here we report cryo-electron microscopy structures of native GlyRs from pig spinal cord and brainstem, revealing structural insights into heteromeric receptors and their predominant subunit stoichiometry of 4α:1β. Within the heteromeric pentamer, the β(+)-α(-) interface adopts a structure that is distinct from the α(+)-α(-) and α(+)-β(-

SUBMITTER: Zhu H 

PROVIDER: S-EPMC8647860 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature