Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide.
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.
Stern
L J
LJ
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge Massachusetts 62138.
Brown
J H
JH
Jardetzky
T S
TS
Gorga
J C
JC
Urban
R G
RG
Strominger
J L
JL
Wiley
D C
DC
D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D015798:HLA-DR1 Antigen / Q000737:chemistry* / Q000378:metabolism; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006388:Hemagglutinins / Q000737:chemistry*; D006389:Hemagglutinins, Viral / Q000737:chemistry*; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D011948:Receptors, Antigen, T-Cell / Q000378:metabolism
D015798:HLA-DR1 Antigen; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006388:Hemagglutinins; D006389:Hemagglutinins, Viral; D010446:Peptide Fragments; D011948:Receptors, Antigen, T-Cell; C086595:influenza hemagglutinin (306-318)