Evidence map›Paper›PMID 17901336›Full record

ArticleScience (New York, N.Y.)2007

Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4.

Chih-Chin Huang, Son N Lam, Priyamvada Acharya, Min Tang, Shi-Hua Xiang, Syed Shahzad-Ul Hussan, Robyn L Stanfield, James Robinson, Joseph Sodroski, Ian A Wilson and 3 more

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 248 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
248citing papers in PubMed, 1 pooled it
12.9field-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

248 citing papers in PubMed, 1 synthesis or guideline pooled it, 407 citations in OpenAlex.

  1. Pooled it
  2. FromImmune network · 2026
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  17. ACS chemical biology · 2022
    Article
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  20. Review

188 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

13 authors at 6 institutions in 1 country.

Chih-Chin HuangVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Son N Lam
Priyamvada Acharya
Min Tang
Shi-Hua Xiang
Syed Shahzad-Ul Hussan
Robyn L Stanfield
James Robinson
Joseph Sodroski
Ian A Wilson
Richard Wyatt
Carole A Bewley
Peter D Kwong
Scripps Research Institute · USDana-Farber Cancer Institute · USNational Institute of Diabetes and Digestive and Kidney Diseases · USHarvard University · USNational Institute of Allergy and Infectious Diseases · USNational Institutes of Health · US

Funding

Viral Sequencing CoreU19AI067854 · NIAID · DUKE UNIVERSITY · PI CRUMP, JOHN ANDREW · 2006 to 2011
$290.5M
The impact of HIV viral diversity and cellular immunity on HIV pathogenesisP30AI060354 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI ROBERT A. PARKER · 2004 to 2026
$94.4M
Inhibitors Of Hiv-1 Cell Fusion And Mycothiol-related EnZ01DK032103 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BEWLEY, CAROLE · 2000 to 2008
$896k
Neutralization Mechanisms Of HIV-1 Monoclonal AntibodiesZ01AI005022 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI KWONG, PETER D · 2002 to 2008
$733k
Production And Characterization Of HIV-1 Solid Phase ProteoliposomesZ01AI005025 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI WYATT, RICHARD THOMAS · 2002 to 2008
$606k
Intramural NIH HHS Z99 AI999999NIAID NIH HHS P30 AI060354NIAID NIH HHS U19 AI067854
6 · The paper itself

Abstract

The CCR5 co-receptor binds to the HIV-1 gp120 envelope glycoprotein and facilitates HIV-1 entry into cells. Its N terminus is tyrosine-sulfated, as are many antibodies that react with the co-receptor binding site on gp120. We applied nuclear magnetic resonance and crystallographic techniques to analyze the structure of the CCR5 N terminus and that of the tyrosine-sulfated antibody 412d in complex with gp120 and CD4. The conformations of tyrosine-sulfated regions of CCR5 (alpha-helix) and 412d (extended loop) are surprisingly different. Nonetheless, a critical sulfotyrosine on CCR5 and on 412d induces similar structural rearrangements in gp120. These results now provide a framework for understanding HIV-1 interactions with the CCR5 N terminus during viral entry and define a conserved site on gp120, whose recognition of sulfotyrosine engenders posttranslational mimicry by the immune system.

Indexed as

Amino Acid SequenceCD4 AntigensCrystallography, X-RayHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansModels, MolecularMolecular MimicryMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide FragmentsReceptors, CCR5SulfatesTyrosineVirus InternalizationCD4 AntigensHIV AntibodiesHIV Envelope Protein gp120HIV envelope protein gp120 (305-321)Peptide FragmentsReceptors, CCR5SulfatesTyrosine

Identifiers

PMID17901336
PMCPMC2278242
OpenAlexW2024011553

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.