Modular Structure and Polymerization Status of GABA_A Receptors Illustrated with EM Analysis and AlphaFold2 Prediction.

ABSTRACT: Type-A γ-aminobutyric acid (GABA_A) receptors are channel proteins crucial to mediating neuronal balance in the central nervous system (CNS). The structure of GABA_A receptors allows for multiple binding sites and is key to drug development. Yet the formation mechanism of the receptor's distinctive pentameric structure is still unknown. This study aims to investigate the role of three predominant subunits of the human GABA_A receptor in the formation of protein pentamers. Through purifying and refolding the protein fragments of the GABA_A receptor α1, β2, and γ2 subunits, the particle structures were visualised with negative staining electron microscopy (EM). To aid the analysis, AlphaFold2 was used to compare the structures. Results show that α1 and

SUBMITTER: Kan C 

PROVIDER: S-EPMC11432007 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature