Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.65
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
DOI:10.2210/pdb1kg0/pdb
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.
Resolution:2.65
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
DOI:10.2210/pdb1kg0/pdb
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.
| Date made available | 2002 |
|---|---|
| Publisher | RCSB-PDB |