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Two neighboring residues of loop A of the α 1 subunit point towards the benzodiazepine binding site of GABA A receptors
Author(s) -
Tan Kelly R.,
Baur Roland,
Gonthier Anne,
Goeldner Maurice,
Sigel Erwin
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.08.068
Subject(s) - gabaa receptor , chemistry , anxiolytic , cys loop receptors , receptor , binding site , benzodiazepine , stereochemistry , muscle relaxant , diazepam , pharmacology , biochemistry , biology , nicotinic agonist , nicotinic acetylcholine receptor
Benzodiazepines are widely used drugs exerting sedative, anxiolytic, muscle relaxant, and anticonvulsant effects by acting through specific high affinity binding sites on some GABA A receptors. It is important to understand how these ligands are positioned in this binding site. We are especially interested here in the conformation of loop A of the α 1 β 2 γ 2 GABA A receptor containing a key residue for the interaction of benzodiazepines: α 1 H101. We describe a direct interaction of α 1 N102 with a diazepam‐ and an imidazobenzodiazepine‐derivative. Our observations help to better understand the conformation of this region of the benzodiazepine pocket in GABA A receptor.