2MIM

NMR structure of the chicken CD3 epsilon delta/gamma heterodimer


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the least restraint violations 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of the chicken CD3 epsilon delta / gamma heterodimer and its assembly with the alpha beta T cell receptor

Berry, R.Headey, S.J.Call, M.J.McCluskey, J.Tregaskes, C.A.Kaufman, J.Koh, R.Scanlon, M.J.Call, M.E.Rossjohn, J.

(2014) J Biol Chem 289: 8240-8251

  • DOI: https://doi.org/10.1074/jbc.M113.544965
  • Primary Citation of Related Structures:  
    2MIM

  • PubMed 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.


  • Organizational Affiliation

    From the Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, Victoria 3800, Australia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CD3 epsilon protein,CD3 glycoprotein178Gallus gallusMutation(s): 0 
Gene Names: CD3 epsiloncd3ecd3gCD3Dd
UniProt
Find proteins for Q90768 (Gallus gallus)
Explore Q90768 
Go to UniProtKB:  Q90768
Find proteins for P70069 (Gallus gallus)
Explore P70069 
Go to UniProtKB:  P70069
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsQ90768P70069
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the least restraint violations 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-02-12
    Type: Initial release
  • Version 1.1: 2014-02-26
    Changes: Structure summary
  • Version 1.2: 2014-10-22
    Changes: Database references
  • Version 1.3: 2019-01-23
    Changes: Data collection, Database references, Source and taxonomy, Structure summary