1kg0
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Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor HLA-DR1
OverviewOverview
Epstein-Barr virus (EBV) causes infectious mononucleosis, establishes, long-term latent infections, and is associated with a variety of human, tumors. The EBV gp42 glycoprotein binds MHC class II molecules, playing a, critical role in infection of B lymphocytes. EBV gp42 belongs to the, C-type lectin superfamily, with homology to NK receptors of the immune, system. We report the crystal structure of gp42 bound to the human MHC, class II molecule HLA-DR1. The gp42 binds HLA-DR1 using a surface site, that is distinct from the canonical lectin and NK receptor ligand binding, sites. At the canonical ligand binding site, gp42 forms a large, hydrophobic groove, which could interact with other ligands necessary for, EBV entry, providing a mechanism for coupling MHC recognition and membrane, fusion.
About this StructureAbout this Structure
1KG0 is a Protein complex structure of sequences from Homo sapiens and Human herpesvirus 4. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1., Mullen MM, Haan KM, Longnecker R, Jardetzky TS, Mol Cell. 2002 Feb;9(2):375-85. PMID:11864610
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