Evidence map›Paper›PMID 24305054›Full record

ArticleNature2013

Structural mechanism of ligand activation in human GABA(B) receptor.

Yong Geng, Martin Bush, Lidia Mosyak, Feng Wang, Qing R Fan

Abstract read
In one paragraph

Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

94 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Conformational equilibria in the activation of cystine-knot hormone receptors.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structural Basis of GABAAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  9. Article
  10. Cryo-EM structures of ρ1 GABANature communications · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Genetic implication of GABAFrontiers in pharmacology · 2025
    Review
  15. Article
  16. Review
  17. Review
  18. Cleomin Exerts Acute Antinociceptive Effects in Mice via GABAPharmaceuticals (Basel, Switzerland) · 2023
    Article
  19. Article
  20. Article

34 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Yong GengDepartment of Pharmacology, Columbia University, New York, New York 10032, USA.
Martin BushDepartment of Pharmacology, Columbia University, New York, New York 10032, USA.
Lidia MosyakDepartment of Pharmacology, Columbia University, New York, New York 10032, USA.
Feng WangDepartment of Pharmacology, Columbia University, New York, New York 10032, USA.
Qing R Fan1] Department of Pharmacology, Columbia University, New York, New York 10032, USA [2] Department of Pathology & Cell Biology, Columbia University, New York, New York 10032, USA.

Funding

Structural Studies of Metabotropic GABA ReceptorsR01GM088454 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI FAN, QING R · 2009 to 2015
$1.6M
NIGMS NIH HHS R01 GM088454NIGMS NIH HHS R01GM088454
6 · The paper itself

Abstract

Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain. It functions as an obligatory heterodimer of the subunits GBR1 and GBR2. Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms. The apo and antagonist-bound structures represent the resting state of the receptor; the agonist-bound complex corresponds to the active state. Both subunits adopt an open conformation at rest, and only GBR1 closes on agonist-induced receptor activation. The agonists and antagonists are anchored in the interdomain crevice of GBR1 by an overlapping set of residues. An antagonist confines GBR1 to the open conformation of the inactive state, whereas an agonist induces its domain closure for activation. Our data reveal a unique activation mechanism for GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits.

Indexed as

ApoproteinsBinding SitesCrystallography, X-RayDisulfidesGABA-B Receptor AgonistsGABA-B Receptor AntagonistsHumansLigandsModels, MolecularProtein MultimerizationProtein Structure, TertiaryProtein SubunitsReceptors, GABA-BSubstrate SpecificityApoproteinsDisulfidesGABA-B Receptor AgonistsGABA-B Receptor AntagonistsLigandsProtein SubunitsReceptors, GABA-B

Identifiers

PMID24305054
PMCPMC3865065

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.