Open AccessStructure of a SARS coronavirus‐derived peptide bound to the human major histocompatibility complex class I molecule HLA‐B*1501
Author(s) -
Røder Gustav,
Kristensen Ole,
Kastrup Jette S.,
Buus Søren,
Gajhede Michael
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108012396
Subject(s) - human leukocyte antigen , major histocompatibility complex , virology , histocompatibility , coronavirus , covid-19 , peptide , biology , immunology , antigen , medicine , infectious disease (medical specialty) , biochemistry , disease , pathology
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.