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

A picrotoxin-specific conformational change in the glycine receptor M2-M3 loop.

The Journal of biological chemistry - 28 Oct 2005

Hawthorne Rebecca, Lynch Joseph W

Abstract excerpt

The external loop linking the M2 and M3 transmembrane domains is crucial for coupling agonist binding to channel gating in the glycine receptor chloride channel (GlyR). A substituted cysteine accessibility scan previously showed that glycine activation increased the surface accessibility of 6 contiguous residues (Arg271-Lys276) toward the N-terminal end of the homomeric alpha1 GlyR M2-M3 loop. In the present...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Site
Share to Cyclopentanes
Share to Diterpenes

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

Share to Electrophysiology

Share to Furans

Share to Inhibitory Concentration 50

Share to Mesylates

Share to Receptors, Glycine

Source

Identifiers

PMID: 16109711
DOI: 10.1074/jbc.M506645200

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

A picrotoxin-specific conformational change in the glycine receptor M2-M3 loop.PMID 16109711Read ↗

Comparison of taurine- and glycine-induced conformational changes in the M2-M3 domain of the glycine receptor.Semantic proximity Read ↗

Effects of a mutation in the TM2-TM3 linker region of the glycine receptor alpha1 subunit on gating and allosteric modulation.Semantic proximity Read ↗

Mapping a molecular link between allosteric inhibition and activation of the glycine receptor.Semantic proximity Read ↗

Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor.Semantic proximity Read ↗

Gating mechanism of the human α1β GlyR by glycineSemantic proximity Read ↗

Propofol modulation of α1 glycine receptors does not require a structural transition at adjacent subunits that is crucial to agonist-induced activation.Semantic proximity Read ↗

Novel regulatory site within the TM3-4 loop of human recombinant alpha3 glycine receptors determines channel gating and domain structure.Semantic proximity Read ↗

The M4 transmembrane segment contributes to agonist efficacy differences between alpha1 and alpha3 glycine receptors.Semantic proximity Read ↗

Mutations at the M2 and M3 Transmembrane Helices of the GABAARs α1 and β2 Subunits Affect Primarily Late Gating Transitions Including Opening/Closing and Desensitization.Semantic proximity Read ↗

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

Building new function into glycine receptors: a structural model for the activation of the glycine-gated chloride channel.Semantic proximity Read ↗

Chloride-dependent conformational changes in the GlyT1 glycine transporterSemantic proximity Read ↗

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