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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites / immunology
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Crystallography, X-Ray
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HLA-B Antigens / chemistry*
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HLA-B Antigens / genetics
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HLA-B Antigens / immunology
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Histocompatibility Antigens Class I / genetics
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Histocompatibility Antigens Class I / isolation & purification
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Histocompatibility Antigens Class I / metabolism*
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Humans
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Hydrogen Bonding
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Hydrophobic and Hydrophilic Interactions
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Ligands
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Models, Molecular
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Mutagenesis, Site-Directed
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Oligopeptides / chemical synthesis
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Oligopeptides / chemistry
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Oligopeptides / immunology*
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Oligopeptides / isolation & purification
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Oligopeptides / metabolism*
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Protein Binding / immunology
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Protein Structure, Secondary
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Severe acute respiratory syndrome-related coronavirus / chemistry*
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Severe acute respiratory syndrome-related coronavirus / immunology
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Water / chemistry
Substances
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HLA-B Antigens
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Histocompatibility Antigens Class I
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Ligands
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Oligopeptides
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Water