ArticleThe Journal of biological chemistry2014
Structure of the chicken CD3εδ/γ heterodimer and its assembly with the αβT cell receptor.
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 9 papers.
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Who cites it
9 citing papers in PubMed.
- In ovo delivery of carvacrol triggers expression of chemotactic factors, antimicrobial peptides and pro-inflammatory pathways in the yolk sac of broiler chicken embryos.Journal of animal science and biotechnology · 2025Article
- Contribution of the TCRβ Repertoire to Marek's Disease Genetic Resistance in the Chicken.Viruses · 2023Article
- The Chicken Embryo Model: A Novel and Relevant Model for Immune-Based Studies.Frontiers in immunology · 2021Review
- Article
- Integrating Experiment and Theory to Understand TCR-pMHC Dynamics.Frontiers in immunology · 2018Review
- Human γδ T cells augment antigen presentation inMolecular medicine (Cambridge, Mass.) · 2016Article
- 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
- Structural Features of the αβTCR Mechanotransduction Apparatus That Promote pMHC Discrimination.Frontiers in immunology · 2015Review
- Molecular architecture of the αβ T cell receptor-CD3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In mammals, the αβT cell receptor (TCR) signaling complex is composed of a TCRαβ heterodimer that is noncovalently coupled to three dimeric signaling molecules, CD3εδ, CD3εγ, and CD3ζζ. The nature of the TCR signaling complex and subunit arrangement in different species remains unclear however. Here we present a structural and biochemical analysis of the more primitive ancestral form of the TCR signaling complex found in chickens. In contrast to mammals, chickens do not express separate CD3δ and CD3γ chains but instead encode a single hybrid chain, termed CD3δ/γ, that is capable of pairing with CD3ε. The NMR structure of the chicken CD3εδ/γ heterodimer revealed a unique dimer interface that results in a heterodimer with considerable deviation from the distinct side-by-side architecture found in human and murine CD3εδ and CD3εγ. The chicken CD3εδ/γ heterodimer also contains a unique molecular surface, with the vast majority of surface-exposed, nonconserved residues being clustered to a single face of the heterodimer. Using an in vitro biochemical assay, we demonstrate that CD3εδ/γ can assemble with both chicken TCRα and TCRβ via conserved polar transmembrane sites. Moreover, analogous to the human TCR signaling complex, the presence of two copies of CD3εδ/γ is required for ζζ assembly. These data provide insight into the evolution of this critical receptor signaling apparatus.
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