1oke: Difference between revisions

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|PDB= 1oke |SIZE=350|CAPTION= <scene name='initialview01'>1oke</scene>, resolution 2.4&Aring;
|PDB= 1oke |SIZE=350|CAPTION= <scene name='initialview01'>1oke</scene>, resolution 2.4&Aring;
|SITE= <scene name='pdbsite=NG1:Bog+Binding+Site+For+Chain+B'>NG1</scene>
|SITE= <scene name='pdbsite=NG1:Bog+Binding+Site+For+Chain+B'>NG1</scene>
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>
|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oke OCA], [http://www.ebi.ac.uk/pdbsum/1oke PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oke RCSB]</span>
}}
}}


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==About this Structure==
==About this Structure==
1OKE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_type_3 Dengue virus type 3]. This structure supersedes the now removed PDB entry 1OAM. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKE OCA].  
1OKE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2]. This structure supersedes the now removed PDB entry 1OAM. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKE OCA].  


==Reference==
==Reference==
A ligand-binding pocket in the dengue virus envelope glycoprotein., Modis Y, Ogata S, Clements D, Harrison SC, Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):6986-91. Epub 2003 May 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12759475 12759475]
A ligand-binding pocket in the dengue virus envelope glycoprotein., Modis Y, Ogata S, Clements D, Harrison SC, Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):6986-91. Epub 2003 May 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12759475 12759475]
[[Category: Dengue virus type 3]]
[[Category: Dengue virus 2]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Harrison, S C.]]
[[Category: Harrison, S C.]]
[[Category: Modis, Y.]]
[[Category: Modis, Y.]]
[[Category: BOG]]
[[Category: NAG]]
[[Category: class 2 fusion protein]]
[[Category: class 2 fusion protein]]
[[Category: dengue virus]]
[[Category: dengue virus]]
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[[Category: virus/viral protein]]
[[Category: virus/viral protein]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:37 2008''

Revision as of 22:46, 30 March 2008

File:1oke.gif


PDB ID 1oke

Drag the structure with the mouse to rotate
, resolution 2.4Å
Sites:
Ligands: , , ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN IN COMPLEX WITH N-OCTYL-BETA-D-GLUCOSIDE


OverviewOverview

Dengue virus is an emerging global health threat. Its major envelope glycoprotein, E, mediates viral attachment and entry by membrane fusion. A crystal structure of the soluble ectodomain of E from dengue virus type 2 reveals a hydrophobic pocket lined by residues that influence the pH threshold for fusion. The pocket, which accepts a hydrophobic ligand, opens and closes through a conformational shift in a beta-hairpin at the interface between two domains. These features point to a structural pathway for the fusion-activating transition and suggest a strategy for finding small-molecule inhibitors of dengue and other flaviviruses.

About this StructureAbout this Structure

1OKE is a Single protein structure of sequence from Dengue virus 2. This structure supersedes the now removed PDB entry 1OAM. Full crystallographic information is available from OCA.

ReferenceReference

A ligand-binding pocket in the dengue virus envelope glycoprotein., Modis Y, Ogata S, Clements D, Harrison SC, Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):6986-91. Epub 2003 May 20. PMID:12759475

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