3C9N

Crystal Structure of a SARS Corona Virus Derived Peptide Bound to the Human Major Histocompatibility Complex Class I molecule HLA-B*1501

Summary for 3C9N

• Entry DOI: 10.2210/pdb3c9n/pdb
• Related: 1xr8 1xr9
• Descriptor: HLA class I histocompatibility antigen, B-15 alpha chain, Beta-2-microglobulin, Peptide antigen, ... (6 entities in total)
• Functional Keywords: major histocompatibility complex class i, mhc-i, hla-b*1501, sars, glycoprotein, host-virus interaction, immune response, membrane, mhc i, polymorphism, transmembrane, ubl conjugation, disease mutation, glycation, immunoglobulin domain, pyrrolidone carboxylic acid, secreted, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P30464; Secreted . Note=(Microbial infection) In the presence of M: P61769
• Total number of polymer chains: 3
• Total formula weight: 45193.06

Authors

Roder, G.A.,Kristensen, O.,Kastrup, J.S.,Buus, S.,Gajhede, M. (deposition date: 2008-02-18, release date: 2008-02-26, Last modification date: 2024-11-13)

Primary citation

Roder, G.,Kristensen, O.,Kastrup, J.S.,Buus, S.,Gajhede, M.
Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501.
ACTA CRYSTALLOGR.,SECT.F, 64:459-462, 2008

PubMed 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.

PubMed: 18540051
DOI: 10.1107/S1744309108012396

Experimental method

X-RAY DIFFRACTION (1.87 Å)