1oke: Difference between revisions
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Revision as of 16:52, 30 October 2007
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CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN IN COMPLEX WITH N-OCTYL-BETA-D-GLUCOSIDE
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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