1oke
CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN IN COMPLEX WITH N-OCTYL-BETA-D-GLUCOSIDE
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OverviewOverview
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.
About this StructureAbout this Structure
1OKE is a [Single protein] structure of sequence from [Dengue virus type 3] with NAG and BOG as [ligands]. This structure superseeds the now removed PDB entry 1OAM. Structure known Active Site: NG1. Full crystallographic information is available from [OCA].
ReferenceReference
A ligand-binding pocket in the dengue virus envelope glycoprotein., Modis Y, Ogata S, Clements D, Harrison SC, Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):6986-91. Epub 2003 May 20. PMID:12759475
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