1oan: Difference between revisions

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==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.

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==

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[[Category: Dengue virus type 3]]

[[Category: Single protein]]

[[Category: Harrison, S.C.]]

[[Category: Harrison, S C.]]

[[Category: Modis, Y.]]

[[Category: NA]]

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[[Category: membrane fusion]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Dengue virus type 3]]
 [[Category: Single protein]]
-[[Category: Harrison, S.C.]]
+[[Category: Harrison, S C.]]
 [[Category: Modis, Y.]]
 [[Category: NA]]
@@ Line 23: / Line 23: @@
 [[Category: membrane fusion]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:55:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:25 2008''