1ok8: Difference between revisions
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
==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, 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 .. | 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== | ||
1OK8 is a | 1OK8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_type_3 Dengue virus type 3] with NAG and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OK8 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 26: | Line 26: | ||
[[Category: trimer]] | [[Category: trimer]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:31:45 2007'' | ||
Revision as of 14:26, 5 November 2007
|
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 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
Page seeded by OCA on Mon Nov 5 13:31:45 2007