An Altered Position of the α2 Helix of MHC Class I Is Revealed by the Crystal Structure of HLA-B3501

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 Å resolution. Comparison with the crystal structure of the closely related allele HLA B*5301 reveals the struc...

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Bibliographic Details
Published in:Immunity (Cambridge, Mass.) Mass.), 1996-03, Vol.4 (3), p.203-213
Main Authors: Smith, Kathrine J., Reid, Scott W., Stuart, David I., McMichael, Andrew J., Jones, E.Yvonne, Bell, John I.
Format: Article
Language:English
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Summary: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 Å 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 α2 helix.
ISSN:1074-7613
1097-4180
DOI:10.1016/S1074-7613(00)80429-X