1ok8

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|PDB= 1ok8 |SIZE=350|CAPTION= <scene name='initialview01'>1ok8</scene>, resolution 2.00&Aring;
|PDB= 1ok8 |SIZE=350|CAPTION= <scene name='initialview01'>1ok8</scene>, resolution 2.00&Aring;
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ok8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok8 OCA], [http://www.ebi.ac.uk/pdbsum/1ok8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ok8 RCSB]</span>
}}
}}
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==About this Structure==
==About this Structure==
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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].
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1OK8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2]. 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://www.ncbi.nlm.nih.gov/pubmed/14737159 14737159]
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]
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[[Category: Dengue virus type 3]]
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[[Category: Dengue virus 2]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Harrison, S C.]]
[[Category: Harrison, S C.]]
[[Category: Modis, Y.]]
[[Category: Modis, Y.]]
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[[Category: CL]]
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[[Category: class 2 fusion protein,]]
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[[Category: NAG]]
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[[Category: class 2 fusion protein]]
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[[Category: dengue virus]]
[[Category: dengue virus]]
[[Category: flavivirus]]
[[Category: flavivirus]]
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[[Category: trimer]]
[[Category: trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:12:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:36 2008''

Revision as of 19:46, 30 March 2008


PDB ID 1ok8

Drag the structure with the mouse to rotate
, resolution 2.00Å
Sites:
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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 2. 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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