Evidence map›Paper›PMID 28332633›Full record

ArticleScientific reports2017

Structural insights into the nucleotide base specificity of P2X receptors.

Go Kasuya, Yuichiro Fujiwara, Hisao Tsukamoto, Satoshi Morinaga, Satoshi Ryu, Kazushige Touhara, Ryuichiro Ishitani, Yuji Furutani, Motoyuki Hattori, Osamu Nureki

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.6field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Adenosine triphosphate mediates the pain tolerance effect of manual acupuncture at Zusanli (ST36) in mice.Journal of traditional Chinese medicine = Chung i tsa chih ying wen pan · 2024
    Article
  5. Computational prediction andPlant signaling & behavior · 2023
    Article
  6. Article
  7. The P2X1 receptor as a therapeutic target.Purinergic signalling · 2022
    Review
  8. Physiologic roles of P2 receptors in leukocytes.Journal of leukocyte biology · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article
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

10 authors at 4 institutions in 2 countries.

Go KasuyaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo, 113-0032, Japan.
Yuichiro FujiwaraIntegrative Physiology, Department of Physiology, Graduate School of Medicine, Osaka University, 2-2 Yamada-oka, Suita, Osaka, 565-0871, Japan.
Hisao TsukamotoInstitute for Molecular Science, 38 Nishigo-Naka, Myodaiji, Okazaki, 444-8585, Japan.
Satoshi MorinagaDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Satoshi RyuDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Kazushige TouharaDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Ryuichiro IshitaniDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo, 113-0032, Japan.
Yuji FurutaniInstitute for Molecular Science, 38 Nishigo-Naka, Myodaiji, Okazaki, 444-8585, Japan.
Motoyuki HattoriState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan University, 2005 Songhu Road, Yangpu District, Shanghai, 200438, China.
Osamu NurekiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo, 113-0032, Japan.
The University of Tokyo · JPInstitute for Molecular Science · JPOsaka University · JPState Key Laboratory of Genetic Engineering

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P2X receptors are trimeric ATP-gated cation channels involved in diverse physiological processes, ranging from muscle contraction to nociception. Despite the recent structure determination of the ATP-bound P2X receptors, the molecular mechanism of the nucleotide base specificity has remained elusive. Here, we present the crystal structure of zebrafish P2X4 in complex with a weak affinity agonist, CTP, together with structure-based electrophysiological and spectroscopic analyses. The CTP-bound structure revealed a hydrogen bond, between the cytosine base and the side chain of the basic residue in the agonist binding site, which mediates the weak but significant affinity for CTP. The cytosine base is further recognized by two main chain atoms, as in the ATP-bound structure, but their bond lengths seem to be extended in the CTP-bound structure, also possibly contributing to the weaker affinity for CTP over ATP. This work provides the structural insights for the nucleotide base specificity of P2X receptors.

Indexed as

AnimalsBinding SitesCytidine TriphosphateMolecular Docking SimulationProtein BindingReceptors, Purinergic P2XXenopus laevisZebrafishZebrafish ProteinsCytidine TriphosphateReceptors, Purinergic P2XZebrafish Proteins

Identifiers

PMID28332633
PMCPMC5362899
OpenAlexW2601937854

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.