Differential assembly diversifies GABA_A receptor structures and signalling.

ABSTRACT: Type A γ-aminobutyric acid receptors (GABA_ARs) are pentameric ligand-gated chloride channels that mediate fast inhibitory signalling in neural circuits^1,2 and can be modulated by essential medicines including general anaesthetics and benzodiazepines³. Human GABA_AR subunits are encoded by 19 paralogous genes that can, in theory, give rise to 495,235 receptor types. However, the principles that govern the formation of pentamers, the permutational landscape of receptors that may emerge from a subunit set and the effect that this has on GABAergic signalling remain largely unknown. Here we use cryogenic electron microscopy to determine the structures of extrasynaptic GABA_ARs assembled from α4, β3 and δ subunits, and their counterparts incor

SUBMITTER: Sente A 

PROVIDER: S-EPMC7612593 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature