Evidence map›Paper›PMID 24196962›Full record

ArticleThe Journal of biological chemistry2014

T-cell receptor (TCR)-peptide specificity overrides affinity-enhancing TCR-major histocompatibility complex interactions.

David K Cole, Kim M Miles, Florian Madura, Christopher J Holland, Andrea J A Schauenburg, Andrew J Godkin, Anna M Bulek, Anna Fuller, Hephzibah J E Akpovwa, Phillip G Pymm and 6 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

46 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
  2. ImmTAC: A Novel Platform of T-Cell Receptor-Based Soluble Bispecifics.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Review
  4. Molecular basis for antibody recognition of multiple drug-peptide/MHC complexes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

16 authors at 3 institutions in 2 countries.

David K ColeFrom Cardiff University School of Medicine, Heath Park, Cardiff CF14 4XN.
Kim M Miles
Florian Madura
Christopher J Holland
Andrea J A Schauenburg
Andrew J Godkin
Anna M Bulek
Anna Fuller
Hephzibah J E Akpovwa
Phillip G Pymm
Nathaniel Liddy
Malkit Sami
Yi Li
Pierre J Rizkallah
Bent K Jakobsen
Andrew K Sewell
Cardiff University · GBImmunocore (United Kingdom) · GBMedical Research Council · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H001085/1Wellcome Trust 100327Wellcome Trust WT086716MA
6 · The paper itself

Abstract

αβ T-cell receptors (TCRs) engage antigens using complementarity-determining region (CDR) loops that are either germ line-encoded (CDR1 and CDR2) or somatically rearranged (CDR3). TCR ligands compose a presentation platform (major histocompatibility complex (MHC)) and a variable antigenic component consisting of a short "foreign" peptide. The sequence of events when the TCR engages its peptide-MHC (pMHC) ligand remains unclear. Some studies suggest that the germ line elements of the TCR engage the MHC prior to peptide scanning, but this order of binding is difficult to reconcile with some TCR-pMHC structures. Here, we used TCRs that exhibited enhanced pMHC binding as a result of mutations in either CDR2 and/or CDR3 loops, that bound to the MHC or peptide, respectively, to dissect the roles of these loops in stabilizing TCR-pMHC interactions. Our data show that TCR-peptide interactions play a strongly dominant energetic role providing a binding mode that is both temporally and energetically complementary with a system requiring positive selection by self-pMHC in the thymus and rapid recognition of non-self-pMHC in the periphery.

Indexed as

Amino Acid SequenceBinding, CompetitiveComplementarity Determining RegionsCrystallography, X-RayHLA-A2 AntigenHLA AntigensHumansKineticsLigandsModels, MolecularMolecular Sequence DataMutationOligopeptidesPeptidesProtein BindingProtein Structure, TertiaryComplementarity Determining RegionsHLA-A*02:01 antigenHLA-A2 AntigenHLA AntigensLigandsMHC binding peptideOligopeptidesPeptidesReceptors, Antigen, T-CellImmunologyMajor Histocompatibility Complex (MHC)Protein-Protein InteractionsReceptor Structure-FunctionT-cell BiologyT-cell Receptor

Identifiers

PMID24196962
PMCPMC3887192
OpenAlexW2113488569

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.