Photoaffinity Labeling of the Benzodiazepine Binding Site of α1β3γ2 γ-Aminobutyric AcidA Receptors with Flunitrazepam Identifies a Subset of Ligands that Interact Directly with His102 of the α Subunit and Predicts Orientation of These within the Benzodiazepine Pharmacophore-Reference-Cited by-同舟云学术

Photoaffinity Labeling of the Benzodiazepine Binding Site of α1β3γ2 γ-Aminobutyric AcidA Receptors with Flunitrazepam Identifies a Subset of Ligands that Interact Directly with His102 of the α Subunit and Predicts Orientation of These within the Benzodiazepine Pharmacophore

Published:1998-07-01 Issue:1 Volume:54 Page:33-43
ISSN:0026-895X
Container-title:Molecular Pharmacology
language:en
Short-container-title:Mol Pharmacol

Author:

McKernan Ruth M.,Farrar Sophie,Collins Ian,Emms Frances,Asuni Ayodeji,Quirk Kathleen,Broughton Howard

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference40 articles.

1. Two Tyrosine Residues on the α Subunit Are Crucial for Benzodiazepine Binding and Allosteric Modulation of γ-Aminobutyric AcidA Receptors

2. Flunitrazepam photoaffinity labeling of the GABAA receptor reduces inhibition of [3H]Ro15-4513 binding by GABA

3. Subtle Changes in Residue 77 of the γ Subunit of α1β2γ2 GABAA Receptors Drastically Alter the Affinity for Ligands of the Benzodiazepine Binding Site

4. Residues at Positions 206 and 209 of the α1 Subunit of γ-Aminobutyric AcidAReceptors Influence Affinities for Benzodiazepine Binding Site Ligands

5. A point mutation in the 2 subunit of -aminobutyric acid type A receptors results in altered benzodiazepine binding site specificity

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