The crystal structure of H-2Dd MHC class I complexed with the HIV-1-derived peptide P18-I10 at 2.4 A resolution: implications for T cell and NK cell recognition.
The structure of H-2Dd complexed with the HIV-derived peptide P18-I10 (RGPGRAFVTI) has been determined by X-ray crystallography at 2.4 A resolution. This MHC class I molecule has an unusual binding motif with four anchor residues in the peptide (G2, P3, R/K/H5, and I/L/F9 or 10). The cleft architecture of H-2Dd includes a deep narrow passage accomodating the N-terminal part of the peptide, explaining the obligatory G2P3 anchor motif. Toward the C-terminal half of the peptide, p5R to p8V form a type I' reverse turn; residues p6A to p9T, and in particular p7F, are readily exposed. The structure is discussed in relation to functional data available for T cell and natural killer cell recognition of the H-2Dd molecule.
Achour
A
A
Microbiology and Tumor Biology Center, Karolinska Hospital, Stockholm, Sweden.
Persson
K
K
Harris
R A
RA
Sundbäck
J
J
Sentman
C L
CL
Lindqvist
Y
Y
Schneider
G
G
Kärre
K
K
D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D000939:Epitopes / Q000737:chemistry; D006183:H-2 Antigens / Q000737:chemistry* / Q000378:metabolism; D019302:HIV Envelope Protein gp160 / Q000737:chemistry*; D064532:Histocompatibility Antigen H-2D; D015395:Histocompatibility Antigens Class I / Q000737:chemistry* / Q000378:metabolism; D007694:Killer Cells, Natural / Q000276:immunology / Q000378:metabolism; D008024:Ligands; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012997:Solvents; D013601:T-Lymphocytes / Q000276:immunology
D000939:Epitopes; D006183:H-2 Antigens; D019302:HIV Envelope Protein gp160; D064532:Histocompatibility Antigen H-2D; D015395:Histocompatibility Antigens Class I; D008024:Ligands; D010455:Peptides; D012997:Solvents