Crystal structure of glycoprotein B from herpes simplex virus 1
- PMID: 16840698
- DOI: 10.1126/science.1126548
Crystal structure of glycoprotein B from herpes simplex virus 1
Abstract
Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An alpha-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended beta hairpins with hydrophobic tips, homologous to fusion peptides in VSV G, relate gB to class II fusion proteins. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. The domain connectivity within a gB monomer would permit such a rearrangement, including long-range translocations linked to viral and cellular membranes.
Comment in
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Biochemistry. Viral glycoproteins and an evolutionary conundrum.Science. 2006 Jul 14;313(5784):177-8. doi: 10.1126/science.1129761. Science. 2006. PMID: 16840685 No abstract available.
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