Evidence map›Paper›PMID 19641588›Full record

ArticleNature2009

Crystal structure of the ATP-gated P2X(4) ion channel in the closed state.

Toshimitsu Kawate, Jennifer Carlisle Michel, William T Birdsong, Eric Gouaux

Open access · greenAbstract read
In one paragraph

Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 383 papers.

0numbers the graph read from it
0cells of the map it votes in
383citing papers in PubMed
46.5field-weighted citation impact, top 1% of its field
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

383 citing papers in PubMed, 731 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Possible Roles for Purinergic Receptor P2RX4 in Breast and Prostate Cancers.International journal of molecular sciences · 2025
    Review
  15. Subtype-specific structural features of the hearing loss-associated human P2X2 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. Review
  18. Species Differences of P2X4 Receptor Modulators.ACS pharmacology & translational science · 2025
    Article
  19. Article
  20. Review

323 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

4 authors at 2 institutions in 1 country.

Toshimitsu KawateVollum Institute, Oregon Health and Science University, 3181 Southwest Sam Jackson Park Road, Oregon 97239, USA.
Jennifer Carlisle Michel
William T Birdsong
Eric Gouaux
Vollum Institute · USOregon Health & Science University · US

Funding

Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI HENDRICKSON, WAYNE A. · 2005 to 2009
$16.8M
Howard Hughes Medical InstituteNIGMS NIH HHS U54 GM075026
6 · The paper itself

Abstract

P2X receptors are cation-selective ion channels gated by extracellular ATP, and are implicated in diverse physiological processes, from synaptic transmission to inflammation to the sensing of taste and pain. Because P2X receptors are not related to other ion channel proteins of known structure, there is at present no molecular foundation for mechanisms of ligand-gating, allosteric modulation and ion permeation. Here we present crystal structures of the zebrafish P2X(4) receptor in its closed, resting state. The chalice-shaped, trimeric receptor is knit together by subunit-subunit contacts implicated in ion channel gating and receptor assembly. Extracellular domains, rich in beta-strands, have large acidic patches that may attract cations, through fenestrations, to vestibules near the ion channel. In the transmembrane pore, the 'gate' is defined by an approximately 8 A slab of protein. We define the location of three non-canonical, intersubunit ATP-binding sites, and suggest that ATP binding promotes subunit rearrangement and ion channel opening.

Indexed as

Models, MolecularAdenosine TriphosphateAnimalsBinding SitesCell LineCrystallography, X-RayGadoliniumHumansIon ChannelsMembrane ProteinsProtein BindingProtein FoldingProtein Structure, TertiaryPurinergic P2 Receptor AntagonistsReceptors, Purinergic P2Receptors, Purinergic P2X4Adenosine TriphosphateGadoliniumIon ChannelsMembrane ProteinsP2RX4 protein, humanPurinergic P2 Receptor AntagonistsReceptors, Purinergic P2Receptors, Purinergic P2X4Zebrafish Proteins

Identifiers

PMID19641588
PMCPMC2720809
OpenAlexW2099163813

What OpenQuestion holds

Textmetadata
LicenceTDM
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.