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*
Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford, United Kingdom;
Structural Biology Center, National Institute of Genetics, Mishima, Shizuoka, Japan;
Division of Viral Immunology, Center for AIDS Research, Kumamoto University, Honjo, Kumamoto, Japan; and
§
Oxford Center for Molecular Sciences, New Chemistry Building, Oxford, United Kingdom
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 
1-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.
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