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

Stoichiometry of a pore mutation that abolishes picrotoxin-mediated antagonism of the GABAA receptor.

The Journal of physiology - 1 Dec 2006

Sedelnikova Anna, Erkkila Brian E, Harris Holly, Zakharkin Stanislav O, Weiss David S

Abstract excerpt

Picrotoxin, a potent antagonist of the inhibitory central nervous system GABAA and glycine receptors, is believed to interact with residues that line the central ion pore. These pore-lining residues are in the second transmembrane domain (TM2) of each of the five constituent subunits. One of these amino acids, a threonine at the 6' location, when mutated to phenylalanine, abolishes picrotoxin sensitivity. It has...

Read the complete abstract on PubMed

Topics

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

Share to GABA Antagonists
Share to Membrane Potentials

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Microinjections

Share to Nonlinear Dynamics

Share to Patch-Clamp Techniques

Share to Protein Structure, Quaternary

Share to Receptors, GABA-A

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 16990398
DOI: 10.1113/jphysiol.2006.120287
PMCID: PMC1890441

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Stoichiometry of a pore mutation that abolishes picrotoxin-mediated antagonism of the GABAA receptor.PMID 16990398Read ↗

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

Stoichiometric analysis of the TM2 6' phenylalanine mutation on desensitization in alpha1beta2 and alpha1beta2gamma2 GABA A receptors.Semantic proximity Read ↗

Stoichiometry of recombinant heteromeric glycine receptors revealed by a pore-lining region point mutation.Semantic proximity Read ↗

Gephyrin-mediated γ-aminobutyric acid type A and glycine receptor clustering relies on a common binding site.Semantic proximity Read ↗

Partial agonism of taurine at gamma-containing native and recombinant GABAA receptors.Semantic proximity Read ↗

Stoichiometry for α-bungarotoxin block of α7 acetylcholine receptors.Semantic proximity Read ↗

Mutations affecting the glycine receptor agonist transduction mechanism convert the competitive antagonist, picrotoxin, into an allosteric potentiator.Semantic proximity Read ↗

Structural model for gamma-aminobutyric acid receptor noncompetitive antagonist binding: widely diverse structures fit the same site.Semantic proximity Read ↗

A conserved tyrosine in the beta2 subunit M4 segment is a determinant of gamma-aminobutyric acid type A receptor sensitivity to propofol.Semantic proximity Read ↗

GABAA receptor cysteinyl mutants and the ginkgo terpenoid lactones bilobalide and ginkgolides.Semantic proximity Read ↗

Functional sites involved in modulation of the GABAA receptor channel by the intravenous anesthetics propofol, etomidate and pentobarbital.Semantic proximity Read ↗

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