2h6o

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Revision as of 18:15, 29 January 2008

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spinqualitylabelsall models 2h6o, resolution 3.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 with , , , , and as ligands. 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

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