Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural requirements for ligand interactions at the benzodiazepine recognition site of the GABA(A) receptor.

Journal of neurochemistry - 1 May 1998

Davies M, Bateson A N, Dunn S M

Abstract excerpt

His101 of the GABA(A) receptor alpha1 subunit is an important determinant of benzodiazepine recognition and a major site of photolabeling by [3H]flunitrazepam. To investigate further the chemical specificity of the residue in this position, we substituted it with phenylalanine, tyrosine, lysine, glutamate, glutamine, or cysteine. The mutant alpha subunits were coexpressed with the rat beta2 and gamma2 subunits in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Azides
Share to Benzodiazepines
Share to Cell Line

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Mutation

Share to Receptors, GABA-A

Source

Identifiers

PMID: 9572307
DOI: 10.1046/j.1471-4159.1998.70052188.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural requirements for ligand interactions at the benzodiazepine recognition site of the GABA(A) receptor.PMID 9572307Read ↗

Role of the histidine residue at position 105 in the human alpha 5 containing GABA(A) receptor on the affinity and efficacy of benzodiazepine site ligands.Semantic proximity Read ↗

Determinants of antagonist binding at the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor subunit, GluR-D. Role of the conserved arginine 507 and glutamate 727 residues.Semantic proximity Read ↗

Engineered Flumazenil Recognition Site Provides Mechanistic Insight Governing Benzodiazepine Modulation in GABAA Receptors.Semantic proximity Read ↗

Mechanism of alpha-subunit selectivity of benzodiazepine pharmacology at gamma-aminobutyric acid type A receptors.Semantic proximity Read ↗

The alpha5(H105R) mutation impairs alpha5 selective binding properties by altered positioning of the alpha5 subunit in GABAA receptors containing two distinct types of alpha subunits.Semantic proximity Read ↗

Agonist-specific conformational changes in the α1-γ2 subunit interface of the GABA A receptor.Semantic proximity Read ↗

Propofol Is an Allosteric Agonist with Multiple Binding Sites on Concatemeric Ternary GABAA Receptors.Semantic proximity Read ↗

Characterization of benzodiazepine binding site on human alpha1-acid glycoprotein using flunitrazepam as a photolabeling agent.Semantic proximity Read ↗

Three arginines in the GABAA receptor binding pocket have distinct roles in the formation and stability of agonist- versus antagonist-bound complexes.Semantic proximity Read ↗

A single point mutation of the GABA(A) receptor alpha5-subunit confers fluoxetine sensitivity.Semantic proximity Read ↗

Natural mutation of GABAA receptor alpha 6 subunit alters benzodiazepine affinity but not allosteric GABA effects.Semantic proximity Read ↗

GABA(A) receptor beta 2 Tyr97 and Leu99 line the GABA-binding site. Insights into mechanisms of agonist and antagonist actions.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.