1ok8
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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 ... [(full description)]
About this StructureAbout this Structure
1OK8 is a [Single protein] structure of sequence from [Dengue virus type 3] with NAG and CL as [ligands]. Structure known Active Site: AC1. 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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