Summary
PDB 1DLH deposited: 1994-02-15 modified: 2011-07-13
Title CRYSTAL STRUCTURE OF THE HUMAN CLASS II MHC PROTEIN HLA-DR1 COMPLEXED WITH AN INFLUENZA VIRUS PEPTIDE
Authors Brown, J.H., Gorga, J.C., Jardetzky, T.S., Stern, L.J., Strominger, J.L., Urban, R.G., Wiley, D.C.
Method X-RAY DIFFRACTION
Structure factors resolution 2.8 rfactor 0.205 rfree 0.304
DPI 1.58 theoretical min: 0.57
Citations

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.

Nature. 1994 Mar 17;368(6468):215-21.

Cross References
Database source Identifier Description
PubMed 8145819 NATUAS
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1DLH/1 1DLH 1 hexamer 0 6 8 6240