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- W2022376080 abstract "γ-Aminobutyric acid type A and glycine receptors (GABAARs, GlyRs) are the major inhibitory neurotransmitter receptors and contribute to many synaptic functions, dysfunctions and human diseases. GABAARs are important drug targets regulated by direct interactions with the scaffolding protein gephyrin. Here we deduce the molecular basis of this interaction by chemical, biophysical and structural studies of the gephyrin–GABAAR α3 complex, revealing that the N-terminal region of the α3 peptide occupies the same binding site as the GlyR β subunit, whereas the C-terminal moiety, which is conserved among all synaptic GABAAR α subunits, engages in unique interactions. Thermodynamic dissections of the gephyrin–receptor interactions identify two residues as primary determinants for gephyrin’s subunit preference. This first structural evidence for the gephyrin-mediated synaptic accumulation of GABAARs offers a framework for future investigations into the regulation of inhibitory synaptic strength and for the development of mechanistically and therapeutically relevant compounds targeting the gephyrin–GABAAR interaction. Gephyrin is an adaptor molecule that binds to both GABAA receptors and glycine receptors. Here Maric et al. present the structure between gephyrin and a peptide from GABAAreceptor and identify key residues dictating the preference of gephyrin for glycine receptor." @default.
- W2022376080 created "2016-06-24" @default.
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- W2022376080 date "2014-12-22" @default.
- W2022376080 modified "2023-09-26" @default.
- W2022376080 title "Molecular basis of the alternative recruitment of GABAA versus glycine receptors through gephyrin" @default.
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- W2022376080 doi "https://doi.org/10.1038/ncomms6767" @default.
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