1ok8: Difference between revisions
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[[Image:1ok8.gif|left|200px]] | [[Image:1ok8.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN IN THE POSTFUSION CONFORMATION''' | {{Structure | ||
|PDB= 1ok8 |SIZE=350|CAPTION= <scene name='initialview01'>1ok8</scene>, resolution 2.00Å | |||
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN IN THE POSTFUSION CONFORMATION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OK8 is a [ | 1OK8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_type_3 Dengue virus type 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK8 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14737159 14737159] | ||
[[Category: Dengue virus type 3]] | [[Category: Dengue virus type 3]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trimer]] | [[Category: trimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:12:06 2008'' | ||
Revision as of 14:12, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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