2h6o
From Proteopedia
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| , resolution 3.5Å | |||||||
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| Ligands: | , , , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Epstein Barr Virus Major Envelope Glycoprotein
Overview
Epstein-Barr virus (EBV) infection of B cells is associated with lymphoma and other human cancers. EBV infection is initiated by the binding of the viral envelope glycoprotein (gp350) to the cell surface receptor CR2. We determined the X-ray structure of the highly glycosylated gp350 and defined the CR2 binding site on gp350. Polyglycans shield all but one surface of the gp350 polypeptide, and we demonstrate that this glycan-free surface is the receptor-binding site. Deglycosylated gp350 bound CR2 similarly to the glycosylated form, suggesting that glycosylation is not important for receptor binding. Structure-guided mutagenesis of the glycan-free surface disrupted receptor binding as well as binding by a gp350 monoclonal antibody, a known inhibitor of virus-receptor interactions. These results provide structural information for developing drugs and vaccines to prevent infection by EBV and related viruses.
About this Structure
2H6O is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
Structure of the Epstein-Barr virus major envelope glycoprotein., Szakonyi G, Klein MG, Hannan JP, Young KA, Ma RZ, Asokan R, Holers VM, Chen XS, Nat Struct Mol Biol. 2006 Nov;13(11):996-1001. Epub 2006 Oct 29. PMID:17072314
Page seeded by OCA on Thu Mar 20 17:13:17 2008
Categories: Human herpesvirus 4 | Single protein | Chen, X S. | BMA | FUC | GAL | MAN | NAG | NDG | Glycoprotein
