Asymmetric gating of a human hetero-pentameric glycine receptor.

ABSTRACT: Hetero-pentameric Cys-loop receptors constitute a major type of neurotransmitter receptors that enable signal transmission and processing in the nervous system. Despite intense investigations in their working mechanism and pharmaceutical potentials, how neurotransmitters activate these receptors remain unclear due to the lack of high-resolution structural information in the activated open state. Here we report near-atomic resolution structures in all principle functional states of the human α1β GlyR, which is a major Cys-loop receptor that mediates inhibitory neurotransmission in the central nervous system of adults. Glycine binding induced cooperative and symmetric structural rearrangements in the neurotransmitter-binding extracellular domain, but asymmetrical pore dilation in the transme

SUBMITTER: Liu X 

PROVIDER: S-EPMC9882600 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature