1dlh
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CRYSTAL STRUCTURE OF THE HUMAN CLASS II MHC PROTEIN HLA-DR1 COMPLEXED WITH AN INFLUENZA VIRUS PEPTIDE
OverviewOverview
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.
About this StructureAbout this Structure
1DLH is a Protein complex structure of sequences from [1] with NAG and NDG as ligands. The following page contains interesting information on the relation of 1DLH with [Major Histocompatibility Complex]. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide., Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, Strominger JL, Wiley DC, Nature. 1994 Mar 17;368(6468):215-21. PMID:8145819
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