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PDBsum entry 1dlh
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Histocompatibility antigen
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PDB id
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1dlh
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Contents |
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180 a.a.
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188 a.a.
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13 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the human class ii mhc protein hla-Dr1 complexed with an influenza virus peptide.
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Authors
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L.J.Stern,
J.H.Brown,
T.S.Jardetzky,
J.C.Gorga,
R.G.Urban,
J.L.Strominger,
D.C.Wiley.
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Ref.
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Nature, 1994,
368,
215-221.
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PubMed id
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Abstract
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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 provide a universal mode of peptide binding, distinct from the
strategy used by class I histocompatibility proteins.
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Secondary reference #1
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Title
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Three-Dimensional structure of the human class ii histocompatibility antigen hla-Dr1.
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Authors
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J.H.Brown,
T.S.Jardetzky,
J.C.Gorga,
L.J.Stern,
R.G.Urban,
J.L.Strominger,
D.C.Wiley.
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Ref.
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Nature, 1993,
364,
33-39.
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PubMed id
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