5EB9

Crystal Structure Of Chicken CD8aa Homodimer


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.01 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.237 
  • R-Value Observed: 0.238 

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Literature

The structural basis of chicken, swine and bovine CD8 alpha alpha dimers provides insight into the co-evolution with MHC I in endotherm species.

Liu, Y.Li, X.Qi, J.Zhang, N.Xia, C.

(2016) Sci Rep 6: 24788-24788

  • DOI: https://doi.org/10.1038/srep24788
  • Primary Citation of Related Structures:  
    5EB9, 5EBG, 5EDX

  • PubMed Abstract: 

    It is unclear how the pivotal molecules of the adaptive immune system (AIS) maintain their inherent characteristics and relationships with their co-receptors over the course of co-evolution. CD8α, a fundamental but simple AIS component with only one immunoglobulin variable (IgV) domain, is a good example with which to explore this question because it can fold correctly to form homodimers (CD8αα) and interact with peptide-MHC I (p/MHC I) with low sequence identities between different species. Hereby, we resolved the crystal structures of chicken, swine and bovine CD8αα. They are typical homodimers consisting of two symmetric IgV domains with distinct species specificities. The CD8αα structures indicated that a few highly conserved residues are important in CD8 dimerization and in interacting with p/MHC I. The dimerization of CD8αα mainly depends on the pivotal residues on the dimer interface; in particular, four aromatic residues provide many intermolecular forces and contact areas. Three residues on the surface of CD8α connecting cavities that formed most of the hydrogen bonds with p/MHC I were also completely conserved. Our data propose that a few key conserved residues are able to ensure the CD8α own structural characteristics despite the great sequence variation that occurs during evolution in endotherms.


  • Organizational Affiliation

    Department of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Beijing 100094, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CD8 alpha chain118Gallus gallusMutation(s): 0 
Gene Names: CD8
UniProt
Find proteins for Q6QR64 (Gallus gallus)
Explore Q6QR64 
Go to UniProtKB:  Q6QR64
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6QR64
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.01 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.237 
  • R-Value Observed: 0.238 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 45.36α = 90
b = 87.063β = 90
c = 70.308γ = 90
Software Package:
Software NamePurpose
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
PHENIXrefinement

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
973 ProjectChina2013CB835302

Revision History  (Full details and data files)

  • Version 1.0: 2016-09-14
    Type: Initial release