1ok8: Difference between revisions
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==Overview== | ==Overview== | ||
Dengue virus enters a host cell when the viral envelope glycoprotein, E, binds to a receptor and responds by conformational rearrangement to the | 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== | ==About this Structure== | ||
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[[Category: Dengue virus type 3]] | [[Category: Dengue virus type 3]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Harrison, S | [[Category: Harrison, S C.]] | ||
[[Category: Modis, Y.]] | [[Category: Modis, Y.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: trimer]] | [[Category: trimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:40 2008'' | ||
Revision as of 15:18, 21 February 2008
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CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN IN THE POSTFUSION CONFORMATION
OverviewOverview
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 StructureAbout this Structure
1OK8 is a Single protein structure of sequence from Dengue virus type 3 with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Structure of the dengue virus envelope protein after membrane fusion., Modis Y, Ogata S, Clements D, Harrison SC, Nature. 2004 Jan 22;427(6972):313-9. PMID:14737159
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