Nonstandard peptide binding revealed by crystal structures of HLA-B*5101 complexed with HIV immunodominant epitopes.

Journal article

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-...

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Authors: Maenaka, K; Maenaka, T; Tomiyama, H; Takiguchi, M; Stuart, D

• Publication status: Published
• Journal: Journal of Immunology
• Volume: 165
• Issue: 6
• Pages: 3260-3267
• Publication date: 2000-09-01
• DOI: 10.4049/jimmunol.165.6.3260
• EISSN: 1550-6606
• ISSN: 0022-1767
• Language: English
• Keywords: Humans; HLA-B Antigens; Models, Molecular; Mice; Immunodominant Epitopes; T-Lymphocytes, Cytotoxic; Cross Reactions; Cytotoxicity Tests, Immunologic; Protein Conformation; Killer Cells, Natural; Amino Acid Motifs; Protein Binding; Computer Simulation; Receptors, Immunologic; HIV-1; Peptide Fragments; Crystallography, X-Ray; Receptors, KIR; Binding Sites; Animals; Cell Line; Macromolecular Substances