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Updated: Jul 4, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule
Gustav Røder1, Ole Kristensen, Jette S Kastrup
1Institute of International Health, Immunology and Microbiology, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen, Denmark. g.roder@immi.ku.dk
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.
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