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The crystal structures of the human MHC class I allele HLA-B*5101 in complex with 8-mer, TAFTIPSI, and 9-mer, LPPVVAKEI, immunodominant peptide epitopes from HIV-1 have been determined by x-ray crystallography. In both complexes, the hydrogen-bonding network in the N-terminal anchor (P1) pocket is rearranged as a result of the replacement of the standard tyrosine with histidine at position 171. This results in a nonstandard positioning of the peptide N terminus, which is recognized by B*5101-restricted T cell clones. Unexpectedly, the P5 peptide residues appear to act as anchors, drawing the peptides unusually deeply into the peptide-binding groove of B51. The unique characteristics of P1 and P5 are likely to be responsible for the zig-zag conformation of the 9-mer peptide and the slow assembly of B*5101. A comparison of the surface characteristics in the alpha1-helix C-terminal region for B51 and other MHC class I alleles highlights mainly electrostatic differences that may be important in determining the specificity of human killer cell Ig-like receptor binding.


Journal article


J Immunol

Publication Date





3260 - 3267


Amino Acid Motifs, Animals, Binding Sites, Cell Line, Computer Simulation, Cross Reactions, Crystallography, X-Ray, Cytotoxicity Tests, Immunologic, HIV-1, HLA-B Antigens, HLA-B51 Antigen, Humans, Immunodominant Epitopes, Killer Cells, Natural, Macromolecular Substances, Mice, Models, Molecular, Peptide Fragments, Protein Binding, Protein Conformation, Receptors, Immunologic, Receptors, KIR, T-Lymphocytes, Cytotoxic