Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
