Two neighboring residues of loop A of the α 1  subunit point towards the benzodiazepine binding site of GABA A  receptors | Zendy

Tan Kelly R. | Zendy; Baur Roland | Zendy; Gonthier Anne | Zendy; Goeldner Maurice | Zendy; Sigel Erwin | Zendy

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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.

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