1oke: Difference between revisions

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{{Seed}}
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{{STRUCTURE_1oke|  PDB=1oke  |  SCENE=  }}  
{{STRUCTURE_1oke|  PDB=1oke  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN IN COMPLEX WITH N-OCTYL-BETA-D-GLUCOSIDE'''
===CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN IN COMPLEX WITH N-OCTYL-BETA-D-GLUCOSIDE===




==Overview==
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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.
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{{ABSTRACT_PUBMED_12759475}}


==About this Structure==
==About this Structure==
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[[Category: Trimer]]
[[Category: Trimer]]
[[Category: Virus/viral protein]]
[[Category: Virus/viral protein]]
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