Structures of three HIV-1 HLA-B*5703-peptide complexes and identification of related HLAs potentially associated with long-term nonprogression.

Journal article

Long-term nonprogression during acute HIV infection has been strongly associated with HLA-B*5701 or HLA-B*5703. In this study, we present the high resolution crystal structures of HLA-B*5703 complexes with three HIV-1 epitopes: ISPRTLNAW (ISP), KAFSPEVIPMF (KAF-11), and KAFSPEVI (KAF-8). These reveal peptide anchoring at position 2 and their C termini. The different peptide lengths and primary sequences are accommodated by variation in the specific contacts made to the HLA-B*5703, flexibility...

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Authors: Stewart-Jones, G; Gillespie, G; Overton, I; Kaul, R; Roche, P

• Publication status: Published
• Journal: Journal of Immunology
• Volume: 175
• Issue: 4
• Pages: 2459-2468
• Publication date: 2005-08-01
• DOI: 10.4049/jimmunol.175.4.2459
• EISSN: 1550-6606
• ISSN: 0022-1767
• Language: English
• Keywords: HIV-1; HLA-B Antigens; Crystallography, X-Ray; Protein Binding; Epitopes, T-Lymphocyte; Recombinant Proteins; Computational Biology; Peptide Fragments; HIV Core Protein p24; Alleles; Hydrogen Bonding; HIV Infections; Acute Disease; Immunodominant Epitopes; Antigen Presentation; Disease Progression; Humans