1KG0 : Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor HLA-DR1

  • Theodore S. Jardetzky (Contributor)
  • Richard M Longnecker (Contributor)
  • Maureen M. Mullen (Contributor)
  • Keith Haan (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Classification:Viral protein/Immune system
Release Date:2002-03-27
Deposition Date:2001-11-25
Revision Date:2008-04-27#2011-07-13#2016-11-23
Molecular Weight:59960.66
Macromolecule Type:Protein
Residue Count:517
Atom Site Count:4228

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.
Date made available2002

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