Evidence map›Paper›PMID 32541785›Full record

ArticleNature communications2020

Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20.

David Jonathan Wasilko, Zachary Lee Johnson, Mark Ammirati, Ye Che, Matthew C Griffor, Seungil Han, Huixian Wu

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed, 1 pooled it
7.6field-weighted citation impact, top 2% 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

63 citing papers in PubMed, 1 synthesis or guideline pooled it, 114 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Structure basis for C-C chemokine receptor 4 modulation by orthosteric and allosteric antagonists.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The multifaceted role of XCL1 in health and disease.Protein science : a publication of the Protein Society · 2025
    Review
  13. Structural insights into CXCR4 modulation and oligomerization.Nature structural & molecular biology · 2025
    Article
  14. Feeder-cell-free system forFrontiers in immunology · 2025
    Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

3 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

7 authors at 1 institution in 1 country.

David Jonathan WasilkoDiscovery Sciences, Medicine Design, Pfizer Worldwide Research and Development, Groton, CT, 06340, USA.
Zachary Lee JohnsonDiscovery Sciences, Medicine Design, Pfizer Worldwide Research and Development, Groton, CT, 06340, USA.
Mark AmmiratiDiscovery Sciences, Medicine Design, Pfizer Worldwide Research and Development, Groton, CT, 06340, USA.ORCID http://orcid.org/0000-0002-9118-9616
Ye CheDiscovery Sciences, Medicine Design, Pfizer Worldwide Research and Development, Groton, CT, 06340, USA.
Matthew C GrifforDiscovery Sciences, Medicine Design, Pfizer Worldwide Research and Development, Groton, CT, 06340, USA.
Seungil HanDiscovery Sciences, Medicine Design, Pfizer Worldwide Research and Development, Groton, CT, 06340, USA.ORCID http://orcid.org/0000-0002-1070-3880
Huixian WuDiscovery Sciences, Medicine Design, Pfizer Worldwide Research and Development, Groton, CT, 06340, USA. huixian.wu@pfizer.com.ORCID http://orcid.org/0000-0003-1357-9747
Pfizer (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chemokines are important protein-signaling molecules that regulate various immune responses by activating chemokine receptors which belong to the G protein-coupled receptor (GPCR) superfamily. Despite the substantial progression of our structural understanding of GPCR activation by small molecule and peptide agonists, the molecular mechanism of GPCR activation by protein agonists remains unclear. Here, we present a 3.3-Å cryo-electron microscopy structure of the human chemokine receptor CCR6 bound to its endogenous ligand CCL20 and an engineered Go. CCL20 binds in a shallow extracellular pocket, making limited contact with the core 7-transmembrane (TM) bundle. The structure suggests that this mode of binding induces allosterically a rearrangement of a noncanonical toggle switch and the opening of the intracellular crevice for G protein coupling. Our results demonstrate that GPCR activation by a protein agonist does not always require substantial interactions between ligand and the 7TM core region.

Indexed as

Chemokine CCL20Cryoelectron MicroscopyHumansLigandsProtein BindingReceptors, CCR6Receptors, G-Protein-CoupledSignal TransductionCCL20 protein, humanCCR6 protein, humanChemokine CCL20LigandsReceptors, CCR6Receptors, G-Protein-Coupled

Identifiers

PMID32541785
PMCPMC7295996
OpenAlexW3035444582

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.