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2gum
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(New page: 200px<br /><applet load="2gum" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gum, resolution 2.10Å" /> '''Crystal structure of...)
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Revision as of 09:16, 21 November 2007
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Crystal structure of the extracellular domain of glycoprotein B from Herpes Simplex Virus type I
Overview
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.
About this Structure
2GUM is a Single protein structure of sequence from Human herpesvirus 4 with NA as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of glycoprotein B from herpes simplex virus 1., Heldwein EE, Lou H, Bender FC, Cohen GH, Eisenberg RJ, Harrison SC, Science. 2006 Jul 14;313(5784):217-20. PMID:16840698
Page seeded by OCA on Wed Nov 21 11:24:02 2007
