Identification of a residue in the γ-aminobutyric acid type A receptor α subunit that differentially affects diazepam-sensitive and -insensitive benzodiazepine site binding

Author:

Derry Jason M. C.,Dunn Susan M. J.,Davies Martin

Publisher

Wiley

Subject

Cellular and Molecular Neuroscience,Biochemistry

Reference36 articles.

1. International Union of Pharmacology XV. Subtypes of γ-aminobutyric acidA receptors: classification on the basis of subunit structure and function;Barnard;Pharmacol. Rev.,1998

2. Molecular dissection of benzodiazepine binding and allosteric coupling using chimeric γ-aminobutyric acidA receptor subunits;Boileau;Mol. Pharmacol.,1998

3. Crystal structure of an Ach-binding protein reveals the ligand-binding domain of nicotinic receptors;Brejc;Nature,2001

4. Point mutations of the α1β2γ2 γ-aminobutyric acidA receptor affecting modulation of the channel by ligands of the benzodiazepine binding site;Buhr;Mol. Pharmacol.,1996

5. Residues at position 206 and 209 of the α1 subunit of γ-aminobutyric acidA receptors influence affinities for benzodiazepine site ligands;Buhr;Mol. Pharmacol.,1997

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