Evidence map›Paper›PMID 25612609›Full record

ArticleScience (New York, N.Y.)2015

Structural biology. Crystal structure of the chemokine receptor CXCR4 in complex with a viral chemokine.

Ling Qin, Irina Kufareva, Lauren G Holden, Chong Wang, Yi Zheng, Chunxia Zhao, Gustavo Fenalti, Huixian Wu, Gye Won Han, Vadim Cherezov and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 211 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
211citing papers in PubMed, 1 pooled it
23.7field-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

211 citing papers in PubMed, 1 synthesis or guideline pooled it, 375 citations in OpenAlex.

  1. Pooled it
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  6. Review
  7. Review
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  15. bioRxiv : the preprint server for biology · 2025
    Article
  16. Article
  17. Article
  18. Structural mechanisms underlying the modulation of CXCR4 by diverse small-molecule antagonists.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Structural insights into CXCR4 modulation and oligomerization.Nature structural & molecular biology · 2025
    Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 1 country.

Ling QinUniversity of California, San Diego, Skaggs School of Pharmacy and Pharmaceutical Sciences, La Jolla, CA 92093, USA.
Irina KufarevaUniversity of California, San Diego, Skaggs School of Pharmacy and Pharmaceutical Sciences, La Jolla, CA 92093, USA. thandel@ucsd.edu stevens@usc.edu ikufareva@ucsd.edu.
Lauren G HoldenUniversity of California, San Diego, Skaggs School of Pharmacy and Pharmaceutical Sciences, La Jolla, CA 92093, USA.
Chong WangDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Yi ZhengUniversity of California, San Diego, Skaggs School of Pharmacy and Pharmaceutical Sciences, La Jolla, CA 92093, USA.
Chunxia ZhaoUniversity of California, San Diego, Skaggs School of Pharmacy and Pharmaceutical Sciences, La Jolla, CA 92093, USA.
Gustavo FenaltiDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Huixian WuDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Gye Won HanDepartment of Chemistry, Bridge Institute. Department of Biological Sciences, Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA.
Vadim CherezovDepartment of Chemistry, Bridge Institute.
Ruben AbagyanUniversity of California, San Diego, Skaggs School of Pharmacy and Pharmaceutical Sciences, La Jolla, CA 92093, USA.
Raymond C StevensDepartment of Chemistry, Bridge Institute. Department of Biological Sciences, Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA. thandel@ucsd.edu stevens@usc.edu ikufareva@ucsd.edu.
Tracy M HandelUniversity of California, San Diego, Skaggs School of Pharmacy and Pharmaceutical Sciences, La Jolla, CA 92093, USA. thandel@ucsd.edu stevens@usc.edu ikufareva@ucsd.edu.
University of California, San Diego · USScripps Research Institute · USUniversity of Southern California · US

Funding

Project 3U54GM094618 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI STEVENS, RAYMOND C · 2010 to 2014
$17.1M
Structure, Dynamics and Activation Mechanisms of Chemokine ReceptorsU01GM094612 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HANDEL, TRACY M · 2010 to 2014
$4.5M
Macromolecular DockingR01GM071872 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ABAGYAN, RUBEN · 2004 to 2017
$4.2M
Chemokine interaction with CXCR4 and ACKR3: structure and activation mechanismsR01GM117424 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HANDEL, TRACY M, KUFAREVA, IRINA · 2016 to 2019
$2.2M
Engineering Chemokine Receptor Signaling Complexes In VitroR01GM081763 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HANDEL, TRACY M · 2009 to 2011
$935k
Synthetic Fabs for Crystallization of Chemokine:Receptor ComplexesR21AI101687 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HANDEL, TRACY M · 2012 to 2013
$415k
NIAID NIH HHS R21 AI101687NIGMS NIH HHS R01 GM071872NIGMS NIH HHS R01 GM081763NIGMS NIH HHS R01 GM117424NIGMS NIH HHS U01 GM094612NIGMS NIH HHS U54 GM094618PHS HHS ACB-12002PHS HHS AGM-12006
6 · The paper itself

Abstract

Chemokines and their receptors control cell migration during development, immune system responses, and in numerous diseases, including inflammation and cancer. The structural basis of receptor:chemokine recognition has been a long-standing unanswered question due to the challenges of structure determination for membrane protein complexes. Here, we report the crystal structure of the chemokine receptor CXCR4 in complex with the viral chemokine antagonist vMIP-II at 3.1 angstrom resolution. The structure revealed a 1:1 stoichiometry and a more extensive binding interface than anticipated from the paradigmatic two-site model. The structure helped rationalize a large body of mutagenesis data and together with modeling provided insights into CXCR4 interactions with its endogenous ligand CXCL12, its ability to recognize diverse ligands, and the specificity of CC and CXC receptors for their respective chemokines.

Indexed as

Amino Acid SequenceChemokine CXCL12ChemokinesCrystallography, X-RayDrug DesignHumansModels, ChemicalMolecular Sequence DataProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationReceptors, CXCR4Structural Homology, ProteinChemokine CXCL12ChemokinesCXCL12 protein, humanCXCR4 protein, humanReceptors, CXCR4vMIP-II

Identifiers

PMID25612609
PMCPMC4362693
OpenAlexW2029479572

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.