ArticleNature2019
Structural basis of assembly of the human T cell receptor-CD3 complex.
Article in Nature, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 198 papers.
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Who cites it
198 citing papers in PubMed.
- High peripheral T cell diversity is associated with lower risk of toxicity and superior response to dual immune checkpoint inhibitor therapy in patients with metastatic NSCLC.Journal for immunotherapy of cancer · 2024Trial
- Computational design of optimized and preferentially paired human TCR constant regions for improved T cell function.Science advances · 2026Article
- Structural T-Cell Receptor Analysis in the Age of Machine Learning.Immunological reviews · 2026Review
- Scalable, generalizable and uncertainty-aware integration of spatial multiomics across diverse modalities and platforms with SCIGMA.Nature genetics · 2026Article
- Clustering of the T-cell receptor complex may facilitate T-cell activation by stretching of CD3ζ cytoplasmic tails.European biophysics journal : EBJ · 2026Article
- The challenge and promise of studying human antigen-specific T cells.Nature reviews. Immunology · 2026Review
- The TCR in CAR T cell therapy: use it or lose it?Cancer gene therapy · 2026Review
- To fret over FRET: Unintended fluorescence energy transfer artifacts and their implications for flow cytometry panel design and interpretation as highlighted by TRBC1/2 assays.Cytometry. Part B, Clinical cytometry · 2026Article
- Multivalent Aptamers: Contemporary Engineering Strategies and Biomedical Applications.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- De novo engineered disulfide bond supersedes native interchain linkage to enhance TCR pairing and anti-tumor efficacy in T cell therapy.Cellular & molecular immunology · 2026Article
- Structure-Function Insights into Immune Receptors Drive Innovation in CAR-T Cell Therapy.Current issues in molecular biology · 2026Review
- Dynamic landscape of peripheral blood lymphocyte subsets in dengue patients: a multimodal single-cell and flow cytometry analysis.BMC infectious diseases · 2026Article
- Membrane-Based Assembly and Interactions in Immune Receptors.Chemical reviews · 2026Review
- Transformative biomechanics and mechanobiology breakthroughs shaping the future of health and medicine.Innovation (Cambridge (Mass.)) · 2026Review
- Leveraging mathematical models to predict and control T-cell activation.PLoS computational biology · 2026Article
- Preclinical Evaluation of AHT-102, a CLDN18.2 × CD3 Bispecific Antibody: Pharmacokinetics, Anti-Tumor Efficacy, Tissue Distribution, and Safety Profile.Drugs in R&D · 2026Article
- Mechanotransduction through T cell receptors: consensus, controversies and future outlooks.Experimental & molecular medicine · 2026Review
- TCRγ constant usage tunes human γδ T cell antigen sensitivity, thymic programming, and peripheral function.Science immunology · 2026Article
- Spatial resolution of the metastatic osteosarcoma tumor microenvironment using immunolabeling across murine, canine and human lung.Journal of translational medicine · 2026Article
- Decoding signaling architectures: CAR versus TCR dynamics in solid tumor immunotherapy.Acta biochimica et biophysica Sinica · 2026Review
138 more citing papers are in PubMed but not listed here.
Corrections and comments
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- Erratum issued
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The αβ T cell receptor (TCR), in association with the CD3γε-CD3δε-CD3ζζ signalling hexamer, is the primary determinant of T cell development and activation, and of immune responses to foreign antigens. The mechanism of assembly of the TCR-CD3 complex remains unknown. Here we report a cryo-electron microscopy structure of human TCRαβ in complex with the CD3 hexamer at 3.7 Å resolution. The structure contains the complete extracellular domains and all the transmembrane helices of TCR-CD3. The octameric TCR-CD3 complex is assembled with 1:1:1:1 stoichiometry of TCRαβ:CD3γε:CD3δε:CD3ζζ. Assembly of the extracellular domains of TCR-CD3 is mediated by the constant domains and connecting peptides of TCRαβ that pack against CD3γε-CD3δε, forming a trimer-like structure proximal to the plasma membrane. The transmembrane segment of the CD3 complex adopts a barrel-like structure formed by interaction of the two transmembrane helices of CD3ζζ with those of CD3γε and CD3δε. Insertion of the transmembrane helices of TCRαβ into the barrel-like structure via both hydrophobic and ionic interactions results in transmembrane assembly of the TCR-CD3 complex. Together, our data reveal the structural basis for TCR-CD3 complex assembly, providing clues to TCR triggering and a foundation for rational design of immunotherapies that target the complex.
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Registered trials
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.