Structural highlights
Publication Abstract from PubMed
The disease dengue (DEN) is caused by four serologically related viruses termed DEN1, DEN2, DEN3 and DEN4. The structure of the ectodomain of the envelope protein has been determined previously for DEN2 and DEN3 viruses. Using NMR spectroscopic methods, we solved the solution structure of domain III (ED3), the receptor-binding domain, of the envelope protein of DEN4 virus, human strain 703-4. The structure shows that the nine amino acid changes in ED3 that separate the sylvatic and human DEN4 strains are surface exposed. Important structural differences between DEN4-rED3 and ED3 domains of DEN2, DEN3 and other flaviviruses are discussed.
Solution structure of the envelope protein domain III of dengue-4 virus.,Volk DE, Lee YC, Li X, Thiviyanathan V, Gromowski GD, Li L, Lamb AR, Beasley DW, Barrett AD, Gorenstein DG Virology. 2007 Jul 20;364(1):147-54. Epub 2007 Mar 29. PMID:17395234[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Volk DE, Lee YC, Li X, Thiviyanathan V, Gromowski GD, Li L, Lamb AR, Beasley DW, Barrett AD, Gorenstein DG. Solution structure of the envelope protein domain III of dengue-4 virus. Virology. 2007 Jul 20;364(1):147-54. Epub 2007 Mar 29. PMID:17395234 doi:http://dx.doi.org/S0042-6822(07)00095-5