Identification of amino acid residues responsible for the α5  subunit binding selectivity of L-655,708, a benzodiazepine binding site ligand at the GABAA receptor

Author:

Casula M. Anna,Bromidge Frances A.,Pillai Gopalan V.,Wingrove Peter B.,Martin Karine,Maubach Karen,Seabrook Guy R.,Whiting Paul J.,Hadingham Karen L.

Publisher

Wiley

Subject

Cellular and Molecular Neuroscience,Biochemistry

Reference23 articles.

1. Two tyrosine residues on the alpha subunit are crucial for benzodiazepine binding and allosteric modulation of gamma-aminobutyric acid (A) receptors;Amin;Mol. Pharmacol.,1997

2. International union of pharmacology. XV. Subtypes of gamma-aminobutyric acid (A) receptors: classification on the basis of subunit structure and receptor function;Barnard;Pharmacol. Rev.,1998

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

4. Structural requirements for ligand interactions at the benzodiazepine recognition site of the GABA(A) receptor;Davies;J. Neurochem.,1998

5. Cloning of cDNA sequences encoding human α2 and α3 γ-aminobutyric acidA receptor subunits and characterization of the benzodiazepine pharmacology of recombinant α1-, α2-, α3-, and α5-containing human γ-aminobutyric acidA receptors;Hadingham;Mol. Pharmacol.,1993a

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