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- W1552082562 abstract "Abstract GABA A receptors are activated via low‐affinity binding sites for the agonists GABA or muscimol. Evidence has been provided that the amino acid residueα 1 F64 located at the β 2 (+)/α 1 (–) subunit interface forms part of this binding site. In radioactive ligand binding studies the agonist [ 3 H]muscimol has been found to interact with the receptor via a high‐affinity binding site. This site has been interpreted as a conformational variant of the low‐affinity site. Alternatively, the high‐affinity binding site has been located to the α 1 (+)/β 2 (–) interface and the homologous residue to α 1 F64, β 2 Y62 has been proposed to constitute an important part of this site. Here we investigated the effect of the point mutation α 1 F64L and the homologous mutation β 2 Y62L on agonist and antagonist binding and functional properties in α 1 β 2 γ 2 GABA A receptors. While the mutation in the α 1 subunit had drastic consequences on all studied properties, including desensitization, the mutation in the β 2 subunit had little consequence. Our observations are relevant for the relative location of high‐ and low‐affinity agonist sites in GABA A receptors." @default.
- W1552082562 created "2016-06-24" @default.
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- W1552082562 date "2003-09-17" @default.
- W1552082562 modified "2023-10-16" @default.
- W1552082562 title "On high- and low-affinity agonist sites in GABAA receptors" @default.
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- W1552082562 doi "https://doi.org/10.1046/j.1471-4159.2003.01982.x" @default.
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