5YMW

Crystal structure of 8-mer peptide from Rous sarcoma virus in complex with BF2*1201


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

An Invariant Arginine in Common with MHC Class II Allows Extension at the C-Terminal End of Peptides Bound to Chicken MHC Class I.

Xiao, J.Xiang, W.Zhang, Y.Peng, W.Zhao, M.Niu, L.Chai, Y.Qi, J.Wang, F.Qi, P.Pan, C.Han, L.Wang, M.Kaufman, J.Gao, G.F.Liu, W.J.

(2018) J Immunol 201: 3084-3095

  • DOI: https://doi.org/10.4049/jimmunol.1800611
  • Primary Citation of Related Structures:  
    5YMV, 5YMW

  • PubMed Abstract: 

    MHC molecules are found in all jawed vertebrates and are known to present peptides to T lymphocytes. In mammals, peptides can hang out either end of the peptide-binding groove of classical class II molecules, whereas the N and C termini of peptides are typically tightly bound to specific pockets in classical class I molecules. The chicken MHC, like many nonmammalian vertebrates, has a single dominantly expressed classical class I molecule encoded by the BF2 locus. We determined the structures of BF2*1201 bound to two peptides and found that the C terminus of one peptide hangs outside of the groove with a conformation much like the peptides bound to class II molecules. We found that BF2*1201 binds many peptides that hang out of the groove at the C terminus, and the sequences and structures of this MHC class I allele were determined to investigate the basis for this phenomenon. The classical class I molecules of mammals have a nearly invariant Tyr (Tyr 84 in humans) that coordinates the peptide C terminus, but all classical class I molecules outside of mammals have an Arg in that position in common with mammalian class II molecules. We find that this invariant Arg residue switches conformation to allow peptides to hang out of the groove of BF2*1201, suggesting that this phenomenon is common in chickens and other nonmammalian vertebrates, perhaps allowing the single dominantly expressed class I molecule to bind a larger repertoire of peptides.


  • Organizational Affiliation

    Key Laboratory of Veterinary Bioproduction and Chemical Medicine of the Ministry of Agriculture, Engineering and Technology Research Center for Beijing Veterinary Peptide Vaccine Design and Preparation, Zhongmu Institutes of China Animal Husbandry Industry Co. Ltd., Beijing 100095, China.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Class I histocompatibility antigen, F10 alpha chain
A, D, G, J
271Gallus gallusMutation(s): 0 
UniProt
Find proteins for P15979 (Gallus gallus)
Explore P15979 
Go to UniProtKB:  P15979
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UniProt GroupP15979
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-2-microglobulin
B, E, H, K
98Gallus gallusMutation(s): 0 
Gene Names: B2M
UniProt
Find proteins for P21611 (Gallus gallus)
Explore P21611 
Go to UniProtKB:  P21611
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UniProt GroupP21611
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  • Reference Sequence

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
LEU-PRO-ALA-CYS-VAL-LEU-GLU-VAL
C, F, I, L
8Rous sarcoma virus - Prague CMutation(s): 0 
UniProt
Find proteins for P00526 (Rous sarcoma virus subgroup C (strain Prague))
Explore P00526 
Go to UniProtKB:  P00526
Entity Groups  
UniProt GroupP00526
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 86.817α = 90
b = 117.268β = 111.21
c = 92.507γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
SCALEPACKdata scaling
SHELXDphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-10-24
    Type: Initial release
  • Version 1.1: 2019-07-31
    Changes: Data collection, Database references