Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide

@article{Stern1994CrystalSO,
  title={Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide},
  author={Lawrence J Stern and Jerry H. Brown and Theodore S. Jardetzky and Joan C. Gorga and Robert G. Urban and Jack Leonard Strominger and Don C. Wiley},
  journal={Nature},
  year={1994},
  volume={368},
  pages={215-221}
}
Abstract An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. Pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide… CONTINUE READING
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