1BII
THE CRYSTAL STRUCTURE OF H-2DD MHC CLASS I IN COMPLEX WITH THE HIV-1 DERIVED PEPTIDE P18-110
Summary for 1BII
Entry DOI | 10.2210/pdb1bii/pdb |
Descriptor | MHC CLASS I H-2DD, BETA-2 MICROGLOBULIN, DECAMERIC PEPTIDE, ... (4 entities in total) |
Functional Keywords | complex (mhc i-peptide), major histocompatibility complex class i dd, transmembrane, glycoprotein, complex (mhc i-peptide) complex, complex (mhc i/peptide) |
Biological source | Mus musculus (house mouse) More |
Cellular location | Membrane; Single-pass type I membrane protein: P01900 Secreted: P01887 |
Total number of polymer chains | 3 |
Total formula weight | 56078.59 |
Authors | Achour, A.,Persson, K.,Harris, R.A.,Sundback, J.,Sentman, C.L.,Lindqvist, Y.,Schneider, G.,Karre, K. (deposition date: 1998-06-11, release date: 1998-10-14, Last modification date: 2024-11-20) |
Primary citation | Achour, A.,Persson, K.,Harris, R.A.,Sundback, J.,Sentman, C.L.,Lindqvist, Y.,Schneider, G.,Karre, K. 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. Immunity, 9:199-208, 1998 Cited by PubMed 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. PubMed: 9729040DOI: 10.1016/S1074-7613(00)80602-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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