Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501

Research output: Contribution to journalJournal articleResearchpeer-review

Gustav Røder, Ole Kristensen, Jette S Kastrup, Søren Buus, Michael Gajhede

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 languageEnglish
JournalActa Crystallographica. Section F : Structural Biology and Crystallization Communications
Volume64
Issue numberPt 6
Pages (from-to)459-62
Number of pages3
ISSN1744-3091
DOIs
Publication statusPublished - 2008

Bibliographical note

Keywords: Binding Sites; Crystallography, X-Ray; HLA-B Antigens; Histocompatibility Antigens Class I; Humans; Hydrogen Bonding; Hydrophobicity; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Oligopeptides; Protein Binding; Protein Structure, Secondary; SARS Virus; Water

ID: 9941869