A ligand-binding pocket in the dengue virus envelope glycoprotein.

ABSTRACT: Dengue 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.

SUBMITTER: Modis Y 

PROVIDER: S-EPMC165817 | biostudies-literature | 2003 Jun

REPOSITORIES: biostudies-literature