1KG0

Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor HLA-DR1

Summary for 1KG0

• Entry DOI: 10.2210/pdb1kg0/pdb
• Descriptor: MHC class II Receptor HLA-DR1, Hemagglutinin HA Peptide, gp42 Protein, ... (5 entities in total)
• Functional Keywords: virus, c-type lectin domain, membrane fusion, mhc, viral protein-immune system complex, viral protein/immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Virion membrane : P01903; Cell membrane; Single-pass type I membrane protein: P04229 P03205
• Total number of polymer chains: 4
• Total formula weight: 59960.66

Authors

Mullen, M.M.,Haan, K.M.,Longnecker, R.,Jardetzky, T.S. (deposition date: 2001-11-25, release date: 2002-03-27, Last modification date: 2024-11-13)

Primary citation

Mullen, M.M.,Haan, K.M.,Longnecker, R.,Jardetzky, T.S.
Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1.
Mol.Cell, 9:375-385, 2002

PubMed Abstract: 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.

PubMed: 11864610
DOI: 10.1016/S1097-2765(02)00465-3

Experimental method

X-RAY DIFFRACTION (2.65 Å)