1dlh
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. 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 Page seeded by OCA on Fri May 2 13:59:12 2008