3PWV

An immmunodominant CTL epitope from rinderpest virus presented by cattle MHC class I molecule N*01801 (BoLA-A11)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.191 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Two distinct conformations of a rinderpest virus epitope presented by bovine major histocompatibility complex class I N*01801: a host strategy to present featured peptides

Li, X.Liu, J.Qi, J.Gao, F.Li, Q.Li, X.Zhang, N.Xia, C.Gao, G.F.

(2011) J Virol 85: 6038-6048

  • DOI: https://doi.org/10.1128/JVI.00030-11
  • Primary Citation of Related Structures:  
    3PWU, 3PWV

  • PubMed Abstract: 

    The presentation of viral peptide epitopes to host cytotoxic T lymphocytes (CTLs) is crucial for adaptive cellular immunity to clear the virus infection, especially for some chronic viral infections. Indeed, hosts have developed effective strategies to achieve this goal. The ideal scenario would be that the peptide epitopes stimulate a broad spectrum of CTL responses with diversified T-cell receptor (TCR) usage (the TCR repertoire). It is believed that a diversified TCR repertoire requires a "featured" peptide to be presented by the host major histocompatibility complex (MHC). A featured peptide can be processed and presented in a number of ways. Here, using the X-ray diffraction method, the crystal structures of an antigenic peptide derived from rinderpest virus presented by bovine MHC class I N*01801 (BoLA-A11) have been solved, and two distinct conformations of the presented peptide are clearly displayed. A detailed analysis of the structure and comparative sequences revealed that the polymorphic amino acid isoleucine 73 (Ile73) is extremely flexible, allowing the MHC groove to adopt different conformations to accommodate the rinderpest virus peptide. This makes the peptide more featured by exposing different amino acids for T-cell recognition. The crystal structures also demonstrated that the N*01801 molecule has an unusually large A pocket, resulting in the special conformation of the P1 residue at the N terminus of the peptide. We propose that this strategy of host peptide presentation might be beneficial for creating a diversified TCR repertoire, which is important for a more-effective CTL response.


  • Organizational Affiliation

    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
MHC class I antigen
A, D
274Bos taurusMutation(s): 0 
Gene Names: LA-A11
UniProt
Find proteins for Q95477 (Bos taurus)
Explore Q95477 
Go to UniProtKB:  Q95477
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ95477
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-2-microglobulin
B, E
98Bos taurusMutation(s): 0 
Gene Names: B2M
UniProt
Find proteins for P01888 (Bos taurus)
Explore P01888 
Go to UniProtKB:  P01888
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01888
Sequence Annotations
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  • Reference Sequence

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
9-mer peptide from Hemagglutinin
C, F
9Rinderpest morbillivirusMutation(s): 0 
UniProt
Find proteins for Q9YKD7 (Rinderpest morbillivirus)
Explore Q9YKD7 
Go to UniProtKB:  Q9YKD7
Entity Groups  
UniProt GroupQ9YKD7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.191 
  • Space Group: P 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 83.905α = 90
b = 83.905β = 90
c = 153.005γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
CNSrefinement
PHENIXrefinement
DENZOdata reduction
HKL-2000data scaling
CNSphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-08-24
    Type: Initial release
  • Version 1.1: 2023-11-01
    Changes: Data collection, Database references, Refinement description