The study of GABA A receptors, which are vital for inhibitory signaling in the brain and are implicated in various neurological treatments, has revealed 12 distinct native subunit assemblies via cryo-electron microscopy. This research addresses discrepancies observed in previous studies, unveiling novel subunit interfaces and detailing the interaction of antiepileptic drugs at the benzodiazepine-binding site. Additional proteomic analysis indicates that auxiliary subunits, like neuroligin 2 and GARLH4, modulate GABA A receptor locations and functions at synapses, thereby enhancing our understanding of their role in pharmacology and signaling in the human brain.
GABA A receptors, critical for fast inhibitory signaling, were studied through cryo-electron microscopy, revealing 12 native subunit assemblies and their structures.
Our work defines the structural basis for GABA A receptor signaling and reveals how drugs interact at a molecular level with these essential brain receptors.
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