ArticleThe Journal of biological chemistry2015
Identification of the Docking Site for CD3 on the T Cell Receptor β Chain by Solution NMR.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Purification, Structural Characterization, and Immunomodulatory Activities of a Glucan fromFoods (Basel, Switzerland) · 2025Article
- The Evolving T Cell Receptor Recognition Code: The Rules Are More Like Guidelines.Immunological reviews · 2025Review
- In situ cell-surface conformation of the TCR-CD3 signaling complex.EMBO reports · 2024Article
- Mechanical control of antigen detection and discrimination by T and B cell receptors.Biophysical journal · 2024Review
- Article
- Article
- Allosteric activation of T cell antigen receptor signaling by quaternary structure relaxation.Cell reports · 2021Article
- Naturally Occurring Genetic Alterations in Proximal TCR Signaling and Implications for Cancer Immunotherapy.Frontiers in immunology · 2021Review
- Peptide-MHC Binding Reveals Conserved Allosteric Sites in MHC Class I- and Class II-Restricted T Cell Receptors (TCRs).Journal of molecular biology · 2020Article
- MHC Restriction: Where Are We Now?Viral immunology · 2020Article
- Structural understanding of T cell receptor triggering.Cellular & molecular immunology · 2020Review
- Review
- MHC binding affects the dynamics of different T-cell receptors in different ways.PLoS computational biology · 2019Article
- NMR: an essential structural tool for integrative studies of T cell development, pMHC ligand recognition and TCR mechanobiology.Journal of biomolecular NMR · 2019Article
- Article
- Peptide-MHC (pMHC) binding to a human antiviral T cell receptor induces long-range allosteric communication between pMHC- and CD3-binding sites.The Journal of biological chemistry · 2018Article
- Understanding the drivers of MHC restriction of T cell receptors.Nature reviews. Immunology · 2018Review
- Subtle changes at the variable domain interface of the T-cell receptor can strongly increase affinity.The Journal of biological chemistry · 2018Article
- The Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling.Frontiers in immunology · 2018Review
- Integrating Experiment and Theory to Understand TCR-pMHC Dynamics.Frontiers in immunology · 2018Review
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Authors and funding
12 authors.
Funding
Abstract
The T cell receptor (TCR)-CD3 complex is composed of a genetically diverse αβ TCR heterodimer associated noncovalently with the invariant CD3 dimers CD3ϵγ, CD3ϵδ, and CD3ζζ. The TCR mediates peptide-MHC recognition, whereas the CD3 molecules transduce activation signals to the T cell. Although much is known about downstream T cell signaling pathways, the mechanism whereby TCR engagement by peptide-MHC initiates signaling is poorly understood. A key to solving this problem is defining the spatial organization of the TCR-CD3 complex and the interactions between its subunits. We have applied solution NMR methods to identify the docking site for CD3 on the β chain of a human autoimmune TCR. We demonstrate a low affinity but highly specific interaction between the extracellular domains of CD3 and the TCR constant β (Cβ) domain that requires both CD3ϵγ and CD3ϵδ subunits. The mainly hydrophilic docking site, comprising 9-11 solvent-accessible Cβ residues, is relatively small (∼400 Å(2)), consistent with the weak interaction between TCR and CD3 extracellular domains, and devoid of glycosylation sites. The docking site is centered on the αA and αB helices of Cβ, which are located at the base of the TCR. This positions CD3ϵγ and CD3ϵδ between the TCR and the T cell membrane, permitting us to distinguish among several possible models of TCR-CD3 association. We further correlate structural results from NMR with mutational data on TCR-CD3 interactions from cell-based assays.
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