Modis, YorgoOgata, StevenClements, DavidHarrison, Stephen C.2019-10-132003Modis, Y., S. Ogata, D. Clements, and S. C. Harrison. 2003. “A Ligand-Binding Pocket in the Dengue Virus Envelope Glycoprotein.” Proceedings of the National Academy of Sciences 100 (12): 6986–91. doi:10.1073/pnas.0832193100.0027-84240744-28311091-6490http://nrs.harvard.edu/urn-3:HUL.InstRepos:41542824Dengue virus is an emerging global health threat. Its major envelope glycoprotein, E, mediates viral attachment and entry by membrane fusion. A crystal structure of the soluble ectodomain of E from dengue virus type 2 reveals a hydrophobic pocket lined by residues that influence the pH threshold for fusion. The pocket, which accepts a hydrophobic ligand, opens and closes through a conformational shift in a beta-hairpin at the interface between two domains. These features point to a structural pathway for the fusion-activating transition and suggest a strategy for finding small-molecule inhibitors of dengue and other flaviviruses.en-USA ligand-binding pocket in the dengue virus envelope glycoproteinJournal Article2019-10-1310.1073/pnas.0832193100