期刊
MOLECULAR CELL
卷 9, 期 2, 页码 375-385出版社
CELL PRESS
DOI: 10.1016/S1097-2765(02)00465-3
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资金
- NCI NIH HHS [CA93444] Funding Source: Medline
- NIGMS NIH HHS [T32GM08061] Funding Source: Medline
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 11 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 11 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.
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