1oan
From Proteopedia
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[[Image:1oan.gif|left|200px]] | [[Image:1oan.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN''' | '''CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN''' | ||
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[[Category: Harrison, S C.]] | [[Category: Harrison, S C.]] | ||
[[Category: Modis, Y.]] | [[Category: Modis, Y.]] | ||
- | [[Category: | + | [[Category: Dengue virus]] |
- | [[Category: | + | [[Category: Flavivirus]] |
- | [[Category: | + | [[Category: Fusion peptide]] |
- | [[Category: | + | [[Category: Low-ph conformational change]] |
- | [[Category: | + | [[Category: Membrane fusion]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:36:02 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 00:36, 3 May 2008
CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN
Overview
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 Structure
1OAN is a Single protein structure of sequence from Dengue virus 2. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 03:36:02 2008