Abstract:
: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.
journal_name
Immunityjournal_title
Immunityauthors
Achour A,Persson K,Harris RA,Sundbäck J,Sentman CL,Lindqvist Y,Schneider G,Kärre Kdoi
10.1016/s1074-7613(00)80602-0subject
Has Abstractpub_date
1998-08-01 00:00:00pages
199-208issue
2eissn
1074-7613issn
1097-4180pii
S1074-7613(00)80602-0journal_volume
9pub_type
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