ArticleProceedings of the National Academy of Sciences of the United States of America2004
Solution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling.
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 56 papers.
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Who cites it
56 citing papers in PubMed.
- Development and Validation of a Rapid Titer Assay for the Oncolytic Virus oHSV2 Expressing a PD-L1/CD3 Bispecific Antibody.Viruses · 2026Article
- Membrane-Based Assembly and Interactions in Immune Receptors.Chemical reviews · 2026Review
- Biophysical and Structural Features of αβT-Cell Receptor Mechanosensing: A Paradigmatic Shift in Understanding T-Cell Activation.Immunological reviews · 2025Review
- In situ cell-surface conformation of the TCR-CD3 signaling complex.EMBO reports · 2024Article
- Bi-specific autoantigen-T cell engagers as targeted immunotherapy for autoreactive B cell depletion in autoimmune diseases.Frontiers in immunology · 2024Article
- Non-Antigenic Modulation of Antigen Receptor (TCR) Cβ-FG Loop Modulates Signalling: Implications of External Factors Influencing T-Cell Responses.International journal of molecular sciences · 2023Article
- Extracellular Galectin 4 Drives Immune Evasion and Promotes T-cell Apoptosis in Pancreatic Cancer.Cancer immunology research · 2023Article
- Article
- T Cell Activation Machinery: Form and Function in Natural and Engineered Immune Receptors.International journal of molecular sciences · 2020Review
- Structural understanding of T cell receptor triggering.Cellular & molecular immunology · 2020Review
- The structural basis of T-cell receptor (TCR) activation: An enduring enigma.The Journal of biological chemistry · 2020Review
- Ultrasmall silica nanoparticles directly ligate the T cell receptor complex.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- NMR: an essential structural tool for integrative studies of T cell development, pMHC ligand recognition and TCR mechanobiology.Journal of biomolecular NMR · 2019Article
- Article
- Integrating Experiment and Theory to Understand TCR-pMHC Dynamics.Frontiers in immunology · 2018Review
- The cytosolic domain of T-cell receptor ζ associates with membranes in a dynamic equilibrium and deeply penetrates the bilayer.The Journal of biological chemistry · 2017Article
- An allosteric site in the T-cell receptor Cβ domain plays a critical signalling role.Nature communications · 2017Article
- A conserved αβ transmembrane interface forms the core of a compact T-cell receptor-CD3 structure within the membrane.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The CD4 and CD3δε Cytosolic Juxtamembrane Regions Are Proximal within a Compact TCR-CD3-pMHC-CD4 Macrocomplex.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Structural Model of the Extracellular Assembly of the TCR-CD3 Complex.Cell reports · 2016Article
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6 authors.
Funding
Abstract
Invariant CD3 subunit dimers (CD3epsilongamma, CD3epsilondelta, and CD3zetazeta) are the signaling components of the alphabeta T cell receptor (TCR). The recently solved structure of murine CD3epsilongamma revealed a unique side-to-side interface and central beta-sheets conjoined between the two C2-set Ig-like ectodomains, with the pairing of the parallel G strands implying a potential concerted piston-type movement for signal transduction. Although CD3gamma and CD3delta each dimerize with CD3epsilon, there are differential CD3 subunit requirements for receptor assembly and signaling among T lineage subpopulations, presumably mandated by structural differences. Here we present the solution structure of the heterodimeric CD3epsilondelta complex. Whereas the CD3epsilon subunit conformation is virtually identical to that in CD3epsilongamma, the CD3delta ectodomain adopts a C1-set Ig fold, with a narrower GFC front face beta-sheet that is more parallel to the ABED back face than those beta-sheets in CD3epsilon and CD3gamma. The dimer interface between CD3delta and CD3epsilon is highly conserved among species and of similar character to that in CD3epsilongamma. Glycosylation sites in CD3delta are arranged such that the glycans may point away from the membrane, consistent with a model of TCR assembly that allows the CD3delta chain to be in close contact with the TCR alpha-chain. This and many other structural and biological features provide a basis for modeling putative TCR/CD3 extracellular domain associations. The fact that the two clusters of transmembrane helices, namely, the three CD3epsilon-CD3gamma-TCRbeta segments and the five CD3epsilon-CD3delta-TCRalpha-CD3zeta-CD3zeta segments, are presumably centered beneath the G strand-paired CD3 heterodimers has important implications for TCR signaling.
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