Evidence map›Paper›PMID 24030490›Full record

ArticleScience (New York, N.Y.)2013

Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex.

Qiuxiang Tan, Ya Zhu, Jian Li, Zhuxi Chen, Gye Won Han, Irina Kufareva, Tingting Li, Limin Ma, Gustavo Fenalti, Jing Li and 9 more

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 343 papers.

0numbers the graph read from it
0cells of the map it votes in
343citing papers in PubMed
35.6field-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

343 citing papers in PubMed, 706 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Antibiotics promote susceptibility tobioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Review
  9. 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
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

19 authors at 1 institution in 1 country.

Qiuxiang TanCAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zuchongzhi Road, Pudong, Shanghai, China 201203.
Ya Zhu
Jian Li
Zhuxi Chen
Gye Won Han
Irina Kufareva
Tingting Li
Limin Ma
Gustavo Fenalti
Jing Li
Wenru Zhang
Xin Xie
Huaiyu Yang
Hualiang Jiang
Vadim Cherezov
Hong Liu
Raymond C Stevens
Qiang Zhao
Beili Wu
Scripps Research Institute · 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 CHANCE, MARK R · 2010 to 2014
$4.5M
Macromolecular DockingR01GM071872 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ABAGYAN, RUBEN · 2004 to 2017
$4.2M
Molecular Mechanism of HIV Entry Mediated by Chemokine Receptor CCR5R01AI100604 · NIAID · SHANGHAI INSTITUTE OF MATERIA MEDICA · PI WU, BEILI · 2012 to 2016
$675k
NIAID NIH HHS R01 AI100604NIGMS NIH HHS R01 GM071872NIGMS NIH HHS U01 GM094612NIGMS NIH HHS U54 GM094618
6 · The paper itself

Abstract

The CCR5 chemokine receptor acts as a co-receptor for HIV-1 viral entry. Here we report the 2.7 angstrom-resolution crystal structure of human CCR5 bound to the marketed HIV drug maraviroc. The structure reveals a ligand-binding site that is distinct from the proposed major recognition sites for chemokines and the viral glycoprotein gp120, providing insights into the mechanism of allosteric inhibition of chemokine signaling and viral entry. A comparison between CCR5 and CXCR4 crystal structures, along with models of co-receptor-gp120-V3 complexes, suggests that different charge distributions and steric hindrances caused by residue substitutions may be major determinants of HIV-1 co-receptor selectivity. These high-resolution insights into CCR5 can enable structure-based drug discovery for the treatment of HIV-1 infection.

Indexed as

Binding SitesCyclohexanesHIV-1HIV Envelope Protein gp120HIV Fusion InhibitorsHumansLigandsMaravirocProtein ConformationReceptors, CCR5Receptors, CXCR4TriazolesVirus InternalizationCXCR4 protein, humanCyclohexanesHIV Envelope Protein gp120HIV Fusion InhibitorsLigandsMaravirocReceptors, CCR5Receptors, CXCR4Triazoles

Identifiers

PMID24030490
PMCPMC3819204
OpenAlexW2146933058

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.