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Crystal structure of a human GABAA receptor

Nature. 2015; 
Miller PS, Aricescu AR
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Peptide Synthesis Resin-bound samples were washed with 10 mM HEPES, pH 7.2, 300 mM NaCl buffer containing detergent at 33 CMC and receptor constructs were eluted overnight in the same buffer supplemented with 500 mM TETSQVAPA peptide (Genscript). Get A Quote

摘要

Type-A γ-aminobutyric acid receptors (GABAARs) are the principal mediators of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signalling triggers hyperactive neurological disorders such as insomnia, anxiety and epilepsy. Here we present the first three-dimensional structure of a GABAAR, the human β3 homopentamer, at 3 Å resolution. This structure reveals architectural elements unique to eukaryotic Cys-loop receptors, explains the mechanistic consequences of multiple human disease mutations and shows an unexpected structural role for a conserved N-linked glycan. The receptor was crystallized bound to a previously unknown agonist, benzamidine, opening a new avenue for the ratio... More

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