An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501.
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.
Smith
K J
KJ
Nuffield Department of Clinical Medicine, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, United Kingdom.
Reid
S W
SW
Stuart
D I
DI
McMichael
A J
AJ
Jones
E Y
EY
Bell
J I
JI
D000483:Alleles; D000595:Amino Acid Sequence; D001483:Base Sequence; D018360:Crystallography, X-Ray; D015693:Gene Products, nef / Q000737:chemistry; D015797:HLA-B35 Antigen / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation
D015693:Gene Products, nef; D015797:HLA-B35 Antigen