The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection.
Solution at 2.4 A resolution of the structure of H-2Db with the influenza virus peptide NP366-374 (ASNEN-METM) and comparison with the H-2Kb-VSV (RGY-VYQGL) structure allow description of the molecular details of MHC class I peptide binding interactions for mice of the H-2b haplotype, revealing a strategy that maximizes the repertoire of peptides than can be presented. The H-2Db cleft has a mouse-specific hydrophobic ridge that causes a compensatory arch in the backbone of the peptide, exposing the arch residues to TCR contact and requiring the peptide to be at least 9 residues. This ridge occurs in about 40% of the known murine D and L allelic molecules, classifying them as a structural subgroup.
Young
A C
AC
Department of Microbiology and Immunology, Albert Einstein College of Medicine, New York, New York 10461.
Zhang
W
W
Sacchettini
J C
JC
Nathenson
S G
SG
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D000939:Epitopes / Q000737:chemistry*; D006183:H-2 Antigens / Q000737:chemistry*; D064532:Histocompatibility Antigen H-2D; D006860:Hydrogen Bonding; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011948:Receptors, Antigen, T-Cell / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction / Q000379:methods
D000939:Epitopes; D006183:H-2 Antigens; D064532:Histocompatibility Antigen H-2D; D009838:Oligodeoxyribonucleotides; D011948:Receptors, Antigen, T-Cell; D011994:Recombinant Proteins