1ok8: Difference between revisions

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==Overview==

Dengue virus enters a host cell when the viral envelope glycoprotein, E, binds to a receptor and responds by conformational rearrangement to the, reduced pH of an endosome. The conformational change induces fusion of, viral and host-cell membranes. A three-dimensional structure of the, soluble E ectodomain (sE) in its trimeric, postfusion state reveals, striking differences from the dimeric, prefusion form. The elongated, trimer bears three 'fusion loops' at one end, to insert into the host-cell, membrane. Their structure allows us to model directly how these fusion, loops interact with a lipid bilayer. The protein folds back on itself, directing its carboxy terminus towards the fusion loops. We propose a, fusion mechanism driven by essentially irreversible conformational changes, in E and facilitated by fusion-loop insertion into the outer bilayer, leaflet. Specific features of the folded-back structure suggest strategies, for inhibiting flavivirus entry.

Dengue virus enters a host cell when the viral envelope glycoprotein, E, binds to a receptor and responds by conformational rearrangement to the reduced pH of an endosome. The conformational change induces fusion of viral and host-cell membranes. A three-dimensional structure of the soluble E ectodomain (sE) in its trimeric, postfusion state reveals striking differences from the dimeric, prefusion form. The elongated trimer bears three 'fusion loops' at one end, to insert into the host-cell membrane. Their structure allows us to model directly how these fusion loops interact with a lipid bilayer. The protein folds back on itself, directing its carboxy terminus towards the fusion loops. We propose a fusion mechanism driven by essentially irreversible conformational changes in E and facilitated by fusion-loop insertion into the outer bilayer leaflet. Specific features of the folded-back structure suggest strategies for inhibiting flavivirus entry.

==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: CL]]

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[[Category: trimer]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Dengue virus enters a host cell when the viral envelope glycoprotein, E, binds to a receptor and responds by conformational rearrangement to the, reduced pH of an endosome. The conformational change induces fusion of, viral and host-cell membranes. A three-dimensional structure of the, soluble E ectodomain (sE) in its trimeric, postfusion state reveals, striking differences from the dimeric, prefusion form. The elongated, trimer bears three 'fusion loops' at one end, to insert into the host-cell, membrane. Their structure allows us to model directly how these fusion, loops interact with a lipid bilayer. The protein folds back on itself, directing its carboxy terminus towards the fusion loops. We propose a, fusion mechanism driven by essentially irreversible conformational changes, in E and facilitated by fusion-loop insertion into the outer bilayer, leaflet. Specific features of the folded-back structure suggest strategies, for inhibiting flavivirus entry.
+Dengue virus enters a host cell when the viral envelope glycoprotein, E, binds to a receptor and responds by conformational rearrangement to the reduced pH of an endosome. The conformational change induces fusion of viral and host-cell membranes. A three-dimensional structure of the soluble E ectodomain (sE) in its trimeric, postfusion state reveals striking differences from the dimeric, prefusion form. The elongated trimer bears three 'fusion loops' at one end, to insert into the host-cell membrane. Their structure allows us to model directly how these fusion loops interact with a lipid bilayer. The protein folds back on itself, directing its carboxy terminus towards the fusion loops. We propose a fusion mechanism driven by essentially irreversible conformational changes in E and facilitated by fusion-loop insertion into the outer bilayer leaflet. Specific features of the folded-back structure suggest strategies for inhibiting flavivirus entry.
 ==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: CL]]
@@ Line 25: / Line 25: @@
 [[Category: trimer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:59:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:40 2008''