1DLH

CRYSTAL STRUCTURE OF THE HUMAN CLASS II MHC PROTEIN HLA-DR1 COMPLEXED WITH AN INFLUENZA VIRUS PEPTIDE

Summary for 1DLH

• Entry DOI: 10.2210/pdb1dlh/pdb
• Descriptor: CLASS II HISTOCOMPATIBILITY ANTIGEN (HLA-DR1) (ALPHA CHAIN), CLASS II HISTOCOMPATIBILITY ANTIGEN (HLA-DR1) (BETA CHAIN), ENTEROTOXIN TYPE B PRECURSOR, ... (6 entities in total)
• Functional Keywords: histocompatibility antigen
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 6
• Total formula weight: 90391.43

Authors

Stern, L.J. (deposition date: 1994-02-15, release date: 1994-06-22, Last modification date: 2020-07-29)

Primary citation

Stern, L.J.,Brown, J.H.,Jardetzky, T.S.,Gorga, J.C.,Urban, R.G.,Strominger, J.L.,Wiley, D.C.
Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide.
Nature, 368:215-221, 1994

PubMed 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 provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.

PubMed: 8145819
DOI: 10.1038/368215a0

Experimental method

X-RAY DIFFRACTION (2.8 Å)