Evidence map›Paper›PMID 22528658›Full record

ArticleProtein science : a publication of the Protein Society2012

Structural basis of interleukin-5 dimer recognition by its α receptor.

Seisuke Kusano, Mutsuko Kukimoto-Niino, Nobumasa Hino, Noboru Ohsawa, Masashi Ikutani, Satoshi Takaki, Kensaku Sakamoto, Miki Hara-Yokoyama, Mikako Shirouzu, Kiyoshi Takatsu and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Impact of TNF and IL-33 Cytokines on Mast Cells in Neuroinflammation.International journal of molecular sciences · 2024
    Review
  6. Article
  7. Article
  8. Challenges and Future Trends in Atopic Dermatitis.International journal of molecular sciences · 2023
    Review
  9. Article
  10. Taking a Breather: Advances in Interleukin 5 Inhibition for Asthma Relief.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Role of the β Common (βc) Family of Cytokines in Health and Disease.Cold Spring Harbor perspectives in biology · 2018
    Review
  18. Article
  19. Elastin-like polypeptide switches: A design strategy to detect multimeric proteins.Protein science : a publication of the Protein Society · 2017
    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

11 authors at 5 institutions in 1 country.

Seisuke KusanoRIKEN Systems and Structural Biology Center, Tsurumi-ku, Yokohama, Japan.
Mutsuko Kukimoto-Niino
Nobumasa Hino
Noboru Ohsawa
Masashi Ikutani
Satoshi Takaki
Kensaku Sakamoto
Miki Hara-Yokoyama
Mikako Shirouzu
Kiyoshi Takatsu
Shigeyuki Yokoyama
Systems Biology Institute · JPNational Center for Global Health and Medicine · JPTokyo Medical and Dental University · JPToyama Prefectural Institute for Pharmaceutical Research · JPUniversity of Toyama · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interleukin-5 (IL-5), a major hematopoietin, stimulates eosinophil proliferation, migration, and activation, which have been implicated in the pathogenesis of allergic inflammatory diseases, such as asthma. The specific IL-5 receptor (IL-5R) consists of the IL-5 receptor α subunit (IL-5RA) and the common receptor β subunit (βc). IL-5 binding to IL-5R on target cells induces rapid tyrosine phosphorylation and activation of various cellular proteins, including JAK1/JAK2 and STAT1/STAT5. Here, we report the crystal structure of dimeric IL-5 in complex with the IL-5RA extracellular domains. The structure revealed that IL-5RA sandwiches the IL-5 homodimer by three tandem domains, arranged in a "wrench-like" architecture. This association mode was confirmed for human cells expressing IL-5 and the full-length IL-5RA by applying expanded genetic code technology: protein photo-cross-linking experiments revealed that the two proteins interact with each other in vivo in the same manner as that in the crystal structure. Furthermore, a comparison with the previously reported, partial GM-CSF•GM-CSFRA•βc structure enabled us to propose complete structural models for the IL-5 and GM-CSF receptor complexes, and to identify the residues conferring the cytokine-specificities of IL-5RA and GM-CSFRA.

Indexed as

Cell LineCrystallography, X-RayHumansInterleukin-5Interleukin-5 Receptor alpha SubunitModels, MolecularProtein BindingProtein ConformationProtein MultimerizationProtein Structure, TertiaryInterleukin-5Interleukin-5 Receptor alpha Subunit

Identifiers

PMID22528658
PMCPMC3403420
OpenAlexW1992948329

What OpenQuestion holds

Textmetadata
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.