The Crystal Structure of H-2Dd MHC Class I Complexed with the HIV-1-Derived Peptide P18-I10 at 2.4 Å Resolution
1998; Cell Press; Volume: 9; Issue: 2 Linguagem: Inglês
10.1016/s1074-7613(00)80602-0
ISSN1097-4180
AutoresAdnane Achour, Karina Persson, Robert A. Harris, Jonas Sundbäck, Charles L. Sentman, Ylva Lindqvist, G. Schneider, Klas Kärre,
Tópico(s)T-cell and B-cell Immunology
ResumoAbstract The structure of H-2D d complexed with the HIV-derived peptide P18-I10 (RGPGRAFVTI) has been determined by X-ray crystallography at 2.4 Å 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-2D d 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-2D d molecule.
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