Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501
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Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501. / Røder, Gustav; Kristensen, Ole; Kastrup, Jette S; Buus, Søren; Gajhede, Michael.
I: Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, Bind 64, Nr. Pt 6, 2008, s. 459-62.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501
AU - Røder, Gustav
AU - Kristensen, Ole
AU - Kastrup, Jette S
AU - Buus, Søren
AU - Gajhede, Michael
N1 - 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
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
U2 - 10.1107/S1744309108012396
DO - 10.1107/S1744309108012396
M3 - Journal article
C2 - 18540051
VL - 64
SP - 459
EP - 462
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
SN - 2053-230X
IS - Pt 6
ER -
ID: 9941869