1ok8
From Proteopedia
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| - | [[Image:1ok8.gif|left|200px]]<br /> | + | [[Image:1ok8.gif|left|200px]]<br /><applet load="1ok8" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ok8" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1ok8, resolution 2.00Å" /> | caption="1ok8, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN IN THE POSTFUSION CONFORMATION'''<br /> | '''CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN IN THE POSTFUSION CONFORMATION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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]. | + | 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]. Known structural/functional Site: <scene name='pdbsite=AC1:Cl Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OK8 OCA]. |
==Reference== | ==Reference== | ||
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[[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 Tue Dec 18 17:48:12 2007'' |
Revision as of 15:38, 18 December 2007
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CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN IN THE POSTFUSION CONFORMATION
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.
About this Structure
1OK8 is a Single protein structure of sequence from Dengue virus type 3 with NAG and CL as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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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