6A6H

Crystal Structure of Swine Major Histocompatibility Complex Class I SLA-2*040202 For 2.3 Angstrom


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.31 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.203 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystallization of SLA-2*04:02:02 complexed with a CTL epitope derived from FMDV.

Ning, S.Wang, Z.B.Qi, P.Xiao, J.Wang, X.J.

(2019) Res Vet Sci 128: 90-98

  • DOI: https://doi.org/10.1016/j.rvsc.2019.11.002
  • Primary Citation of Related Structures:  
    6A6H

  • PubMed Abstract: 

    Presentation of viral epitopes by swine MHC I (termed leukocyte antigen class I, SLA I) to cytotoxic T lymphocytes (CTLs) is crucial for swine immunity. The SLA-2 structure, however, remains largely unknown. To illustrate the structural basis of swine CTL epitope presentation, the crystal structure of SLA-2*04:02:02 complexed with one peptide, derived from foot-and-mouth disease virus (FMDV), was analyzed in this study. SLA-2*04:02:02 and swine β2-microglobulin (sβ2m) were refolded in vitro in the presence of peptides. X-ray diffraction data of SLA-2*04:02:02-peptide-sβ2m (referred to as p/SLA-2*04:02:02) were collected. The diffraction dataset was 2.3 Å in resolution and the space group was P3(2)21. Relevant data included a = 101.8 Å, b = 101.8 Å, c = 73.455 Å,α = 90.00°, β = 90.00°, γ = 120.00°. The structure of p/SLA-2*04:02:02 was analyzed. The results revealed that Glu24, Met68, Gly76, and Gln173 in PBG of SLA-2*04:02:02 are different from other MHC I. Furthermore, Asn63 is different from other SLA I. Gln57, Met174 and Gln180 in PBG of SLA I are different from other species' MHC I. All of these features are different from known mammalian peptide-MHC class I complexes (referred to as p/MHC I). In addition, P4-His, P6-Val, and P8-Pro in the peptide were exposed, and these residues as epitopes can be presented by SLA-2*04:02:02. This study not only provides a structural basis for peptide presentation by SLA-2, but also screens one potential FMDV CTL epitope. The results may be of interest in future vaccine development.


  • Organizational Affiliation

    Key Laboratory of Epidemiology of Ministry of Agriculture, College of Veterinary Medicine, China Agricultural University, 100193 Beijing, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MHC class I antigen275Sus scrofaMutation(s): 0 
Gene Names: SLA-BSLA-2
UniProt
Find proteins for Q8MHU4 (Sus scrofa)
Explore Q8MHU4 
Go to UniProtKB:  Q8MHU4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8MHU4
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-2-microglobulin98Sus scrofaMutation(s): 0 
Gene Names: B2M
UniProt
Find proteins for Q07717 (Sus scrofa)
Explore Q07717 
Go to UniProtKB:  Q07717
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UniProt GroupQ07717
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  • Reference Sequence

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
MET-THR-ALA-HIS-ILE-VAL-VAL-PRO-TYR9Foot-and-mouth disease virus AMutation(s): 0 
UniProt
Find proteins for P49303 (Foot-and-mouth disease virus (isolate -/Azerbaijan/A22-550/1965 serotype A))
Explore P49303 
Go to UniProtKB:  P49303
Entity Groups  
UniProt GroupP49303
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.31 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.203 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 101.802α = 90
b = 101.802β = 90
c = 73.455γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2019-07-03
    Type: Initial release
  • Version 1.1: 2019-10-30
    Changes: Data collection
  • Version 1.2: 2020-01-15
    Changes: Database references
  • Version 1.3: 2023-11-22
    Changes: Data collection, Database references, Refinement description