@article{503fd37d1e9349258cca370d9aeddd2c,
title = "Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1",
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.",
author = "Mullen, {Maureen M.} and Haan, {Keith M.} and Richard Longnecker and Jardetzky, {Theodore S.}",
note = "Funding Information: X-ray data were collected at beamline 5-ID (Dupont-Northwestern-Dow Collaborative Access Team) of the Advanced Photon Source. The authors would like to thank B. Wurzburg and other members of the Jardetzky and Longnecker laboratories for helpful discussions. This work has been supported by grants from the National Institutes of Health (T.S.J. and R.L., CA93444) from the National Cancer Institute, the Pew Scholars Program in the Biomedical Sciences (T.S.J.), and the Cancer Research Institute (T.S.J). R.L. is a Stohlman Scholar and T.S.J. is a Scholar of the Leukemia and Lymphoma Society of America. K.M.H. is supported by the training program in the Cellular and Molecular Basis of Disease (T32 GM08061) from the National Institute of Health. ",
year = "2002",
doi = "10.1016/S1097-2765(02)00465-3",
language = "English (US)",
volume = "9",
pages = "375--385",
journal = "Molecular cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "2",
}