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

Protein mobility and GABA-induced conformational changes in GABA(A) receptor pore-lining M2 segment.

Nature neuroscience - 1 May 2001

Horenstein J, Wagner D A, Czajkowski C, Akabas M H

Abstract excerpt

Protein movements underlying ligand-gated ion channel activation are poorly understood. Here we used disulfide bond trapping to examine the proximity and mobility of cysteines substituted for aligned GABAA receptor alpha1 and beta1 M2 segment channel-lining residues in resting and activated receptors. With or without GABA, disulfide bonds formed at alpha1N275C/beta1E270C (20') and alpha1S272C/beta1H267C (17'),...

Read the complete abstract on PubMed

Topics

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

Share to Disulfides
Share to Electrophysiology
Share to gamma-Aminobutyric Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Oocytes

Share to Patch-Clamp Techniques

Share to Receptors, GABA

Share to Xenopus

Source

Identifiers

PMID: 11319555
DOI: 10.1038/87425

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

Protein mobility and GABA-induced conformational changes in GABA(A) receptor pore-lining M2 segment.PMID 11319555Read ↗

Spontaneous thermal motion of the GABA(A) receptor M2 channel-lining segments.Semantic proximity Read ↗

Loose protein packing around the extracellular half of the GABA(A) receptor beta1 subunit M2 channel-lining segment.Semantic proximity Read ↗

The role of heterogeneity of intersubunit interfaces in the outer membrane leaflet in maintaining GABAA receptor activity.Semantic proximity Read ↗

GABAA receptor subunit M2-M3 linkers have asymmetric roles in pore gating and diazepam modulation.Semantic proximity Read ↗

Substituted Cysteine Modification and Protection with n-Alkyl-MTS Reagents Quantifies Steric Changes Induced by a Mutation in Anesthetic Binding Sites on GABA Type A Receptors.Semantic proximity Read ↗

The pre-M1 segment of the alpha1 subunit is a transduction element in the activation of the GABAA receptor.Semantic proximity Read ↗

A conserved salt bridge critical for GABA(A) receptor function and loop C dynamics.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 ↗

Glycine substitution of α1F64 residue at the loop D of GABAA receptor impairs gating - Implications for importance of binding site-channel gate linker rigidity.Semantic proximity Read ↗

A conformational intermediate in glutamate receptor activation.Semantic proximity Read ↗

Mutation of glutamate 155 of the GABAA receptor beta2 subunit produces a spontaneously open channel: a trigger for channel activation.Semantic proximity Read ↗

Theoretical studies of the M2 transmembrane segment of the glycine receptor: models of the open pore structure and current-voltage characteristics.Semantic proximity Read ↗

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