Evidence map›Paper›PMID 15331779›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

A hairpin turn in a class II MHC-bound peptide orients residues outside the binding groove for T cell recognition.

Zarixia Zavala-Ruiz, Iwona Strug, Bruce D Walker, Philip J Norris, Lawrence J Stern

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

28 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
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  8. Proinsulin C-peptide is an autoantigen in people with type 1 diabetes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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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

5 authors at 3 institutions in 1 country.

Zarixia Zavala-RuizDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Iwona Strug
Bruce D Walker
Philip J Norris
Lawrence J Stern
Harvard University · USMassachusetts General Hospital · USMassachusetts Institute of Technology · US

Funding

Structure and Function of Class II MHC ProteinsR01AI038996 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STERN, LAWRENCE J · 1996 to 2006
$1.6M
CHARACTERIZATION OF HIV-1-SPECIFIC T HELPER CELL CLONESK08AI001698 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI NORRIS, PHILIP J · 2000 to 2004
$598k
Structural studies of the human class II MHC proteins.F31GM064859 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ZAVALA, RUIZ Z · 2001 to 2003
$86k
NIAID NIH HHS K08 AI001698NIAID NIH HHS R01-AI01698NIAID NIH HHS R01 AI038996NIAID NIH HHS R01-AI38996NIGMS NIH HHS F31 GM064859NIGMS NIH HHS F31-GM64859
6 · The paper itself

Abstract

T cells generally recognize peptide antigens bound to MHC proteins through contacts with residues found within or immediately flanking the seven- to nine-residue sequence accommodated in the MHC peptide-binding groove. However, some T cells require peptide residues outside this region for activation, the structural basis for which is unknown. Here, we have investigated a HIV Gag-specific T cell clone that requires an unusually long peptide antigen for activation. The crystal structure of a minimally antigenic 16-mer bound to HLA-DR1 shows that the peptide C-terminal region bends sharply into a hairpin turn as it exits the binding site, orienting peptide residues outside the MHC-binding region in position to interact with a T cell receptor. Peptide truncation and substitution studies show that both the hairpin turn and the extreme C-terminal residues are required for T cell activation. These results demonstrate a previously unrecognized mode of MHC-peptide-T cell receptor interaction.

Indexed as

Lymphocyte ActivationAmino Acid SequenceAntigen PresentationBinding SitesCrystallizationHIV Core Protein p24HLA-DR1 AntigenHumansMolecular Sequence DataPeptide FragmentsProtein ConformationT-LymphocytesHIV Core Protein p24HLA-DR1 AntigenPeptide Fragments

Identifiers

PMID15331779
PMCPMC516560
OpenAlexW2089004428

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.