The domain numbering originally proposed is also indicated [17]. UA represents "hinge" aa not assigned to domains in VSV G in the prior scheme. Sequences with significant WWIHS scores in the fusion domain (II) were identified by MPeX and colored red. Hydrophobic transmembrane domains (violet) were predicted using TMpred. The post fusion secondary structure of VSV G as solved and numbered by Roche and coworkers [17] is depicted with α-helices as cylinders and β-sheets as arrows. The α-helices predicted by PHD In THOV GP and AcMNPV GP64 are indicated similarly. β-sheets (t) and (u) of VSV G are not present in the protein data base structure (2cmz.pdb). In VSV G, α-helices predicted by PHD are indicated by dashed boxes and predicted β-sheets are identified with dashed arrows. Amino acids are numbered beginning after the putative signal sequences enclosed in parentheses. In the alignments (:) refers to identical amino acids. (.) refers to chemically similar amino acids. Plum amino acids: N-glycosylation sites.<p><b>Copyright information:</b></p><p>Taken from "Proteomics computational analyses suggest that baculovirus GP64 superfamily proteins are class III penetrenes"</p><p>http://www.virologyj.com/content/5/1/28</p><p>Virology Journal 2008;5():28-28.</p><p>Published online 18 Feb 2008</p><p>PMCID:PMC2288602.</p><p></p