Abstract
The human leukocyte antigen (HLA) class I system comprises a highly polymorphic set of molecules that specifically bind and present peptides to cytotoxic T cells. HLA-B*1501 is a prototypical member of the HLA-B62 supertype and only two peptide-HLA-B*1501 structures have been determined. Here, the crystal structure of HLA-B*1501 in complex with a SARS coronavirus-derived nonapeptide (VQQESSFVM) has been determined at high resolution (1.87 A). The peptide is deeply anchored in the B and F pockets, but with the Glu4 residue pointing away from the floor in the peptide-binding groove, making it available for interactions with a potential T-cell receptor.
Original language | English |
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Journal | Acta Crystallographica. Section F : Structural Biology and Crystallization Communications |
Volume | 64 |
Issue number | Pt 6 |
Pages (from-to) | 459-62 |
Number of pages | 3 |
ISSN | 1744-3091 |
DOIs | |
Publication status | Published - 2008 |