Summary
PDB 1KG0 deposited: 2001-11-25 modified: 2009-02-24
Title Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor HLA-DR1
Authors Haan, K.M., Jardetzky, T.S., Longnecker, R., Mullen, M.M.
Method X-RAY DIFFRACTION
Structure factors resolution 2.65 rfactor 0.221 rfree 0.247
DPI 1.16 theoretical min: 0.40
Citations

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.

Mol Cell. 2002 Feb;9(2):375-85.

Cross References
Database source Identifier Description
PubMed 11864610 MOCEFL
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1KG0/1 1KG0 1 tetramer 0 4 0 4550