Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B1501
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 c...
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Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2008-06, Vol.64 (6), p.459-462 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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 Å). 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. |
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ISSN: | 1744-3091 1744-3091 |
DOI: | 10.1107/S1744309108012396 |