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 determinants for antagonist pharmacology that distinguish the rho1 GABAC receptor from GABAA receptors.

Molecular pharmacology - 1 Oct 2008

Zhang Jianliang, Xue Fenqin, Chang Yongchang

Abstract excerpt

GABA receptor (GABAR) types C (GABACR) and A (GABAAR) are both GABA-gated chloride channels that are distinguished by their distinct competitive antagonist properties. The structural mechanism underlying these distinct properties is not well understood. In this study, using previously identified binding residues as a guide, we made individual or combined mutations of nine binding residues in the rho1 GABACR...

Read the complete abstract on PubMed

Topics

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

Share to Chloride Channels
Share to GABA Antagonists
Share to Inhibitory Concentration 50

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Organophosphonates

Share to Organophosphorus Compounds

Share to Pyridazines

Share to Receptors, GABA

Share to Receptors, GABA-A

Source

Identifiers

PMID: 18599601
DOI: 10.1124/mol.108.048710

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural determinants for antagonist pharmacology that distinguish the rho1 GABAC receptor from GABAA receptors.PMID 18599601Read ↗

[GABAC receptors: structure and functions].Semantic proximity Read ↗

A single amino acid change within the ion-channel domain of the gamma-aminobutyric acid rho1 receptor accelerates desensitization and increases taurine agonism.Semantic proximity Read ↗

Mutations of the 2' proline in the M2 domain of the human GABAC rho1 subunit alter agonist responses.Semantic proximity Read ↗

Mapping the rho1 GABA(C) receptor agonist binding pocket. Constructing a complete model.Semantic proximity Read ↗

Relative impact of residues at the intracellular and extracellular ends of the human GABAC rho1 receptor M2 domain on picrotoxinin activity.Semantic proximity Read ↗

A Single phenylalanine residue in the main intracellular loop of α1 γ-aminobutyric acid type A and glycine receptors influences their sensitivity to propofol.Semantic proximity Read ↗

Identification of a tyrosine in the agonist binding site of the homomeric rho1 gamma-aminobutyric acid (GABA) receptor that, when mutated, produces spontaneous opening.Semantic proximity Read ↗

The GABAA receptor family: molecular and functional diversity.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 ↗

The GABAA receptors. From subunits to diverse functions.Semantic proximity Read ↗

A single amino acid in the second transmembrane domain of GABA rho receptors regulates channel conductance.Semantic proximity Read ↗

β2E153 Residue at Loop B of GABAAR Is Involved in Agonist Stabilization and Gating Properties.Semantic proximity Read ↗

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