Evidence map›Paper›PMID 37100770›Full record

ArticleNature communications2023

Structural analysis of cancer-relevant TCR-CD3 and peptide-MHC complexes by cryoEM.

Kei Saotome, Drew Dudgeon, Kiersten Colotti, Michael J Moore, Jennifer Jones, Yi Zhou, Ashique Rafique, George D Yancopoulos, Andrew J Murphy, John C Lin and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. 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
11.6field-weighted citation impact, top 2% 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, 42 citations in OpenAlex.

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  12. Three-Dimensional Modeling ofAntibodies (Basel, Switzerland) · 2025
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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

12 authors at 1 institution in 1 country.

Kei SaotomeRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA. kei.saotome@regeneron.com.ORCID 0000-0002-4135-5356
Drew DudgeonRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA.ORCID 0000-0002-2934-0127
Kiersten ColottiRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA.
Michael J MooreRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA.
Jennifer JonesRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA.
Yi ZhouRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA.
Ashique RafiqueRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA.ORCID 0000-0003-4078-7242
George D YancopoulosRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA.
Andrew J MurphyRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA.ORCID 0000-0003-4152-4081
John C LinRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA.
William C OlsonRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA.
Matthew C FranklinRegeneron Pharmaceuticals, Inc., Tarrytown, NY, 10591, USA. matthew.franklin@regeneron.com.ORCID 0000-0002-1482-0136
Regeneron (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The recognition of antigenic peptide-MHC (pMHC) molecules by T-cell receptors (TCR) initiates the T-cell mediated immune response. Structural characterization is key for understanding the specificity of TCR-pMHC interactions and informing the development of therapeutics. Despite the rapid rise of single particle cryoelectron microscopy (cryoEM), x-ray crystallography has remained the preferred method for structure determination of TCR-pMHC complexes. Here, we report cryoEM structures of two distinct full-length α/β TCR-CD3 complexes bound to their pMHC ligand, the cancer-testis antigen HLA-A2/MAGEA4 (230-239). We also determined cryoEM structures of pMHCs containing MAGEA4 (230-239) peptide and the closely related MAGEA8 (232-241) peptide in the absence of TCR, which provided a structural explanation for the MAGEA4 preference displayed by the TCRs. These findings provide insights into the TCR recognition of a clinically relevant cancer antigen and demonstrate the utility of cryoEM for high-resolution structural analysis of TCR-pMHC interactions.

Indexed as

NeoplasmsReceptors, Antigen, T-CellCryoelectron MicroscopyHistocompatibility AntigensHumansMajor Histocompatibility ComplexPeptidesProtein BindingHistocompatibility AntigensPeptidesReceptors, Antigen, T-Cell

Identifiers

PMID37100770
PMCPMC10132440
OpenAlexW4367049975

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.