An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501.

Journal article

The crystal structure of the human major histocompatibility complex class I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution. Comparison with the crystal structure of the closely related allele HLA B*5301 reveals the structural basis for the tyrosine specificity of the B*3501 F pocket. The structure also reveals a novel conformation of the 8-mer peptide within the binding groove. The positions of the peptide N and C termini are nonstandard, but the classic pattern of hydrogen bonding to nonpolymorphic MHC class I residues is maintained, at the N terminus by addition of a water molecule, and at the C terminus by a substantial shift in the alpha 2 helix.

Authors: Smith, K; Reid, S; Stuart, D; McMichael, A; Jones, E

• Publication status: Published
• Journal: Immunity
• Volume: 4
• Issue: 3
• Pages: 203-213
• Publication date: 1996-03-01
• DOI: 10.1016/s1074-7613(00)80429-x
• EISSN: 1097-4180
• ISSN: 1074-7613
• Language: English
• Keywords: Amino Acid Sequence; HLA-B35 Antigen; Crystallography, X-Ray; Base Sequence; Molecular Sequence Data; Models, Molecular; Alleles; Humans; Protein Binding; Gene Products, nef; Protein Conformation