@article{0fa60cf0ebc811ddbf70000ea68e967b,
title = "Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501",
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.",
author = "Gustav R{\o}der and Ole Kristensen and Kastrup, {Jette S} and S{\o}ren Buus and Michael Gajhede",
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",
year = "2008",
doi = "10.1107/S1744309108012396",
language = "English",
volume = "64",
pages = "459--62",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "Pt 6",
}