1oke: Difference between revisions

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==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
1OKE 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 <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=BOG:'>BOG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1OAM. Known structural/functional Site: <scene name='pdbsite=NG1:Bog+Binding+Site+For+Chain+B'>NG1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKE OCA].  
1OKE 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 <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=BOG:'>BOG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1OAM. Known structural/functional Site: <scene name='pdbsite=NG1:Bog+Binding+Site+For+Chain+B'>NG1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKE OCA].  


==Reference==
==Reference==
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[[Category: Dengue virus type 3]]
[[Category: Dengue virus type 3]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Harrison, S.C.]]
[[Category: Harrison, S C.]]
[[Category: Modis, Y.]]
[[Category: Modis, Y.]]
[[Category: BOG]]
[[Category: BOG]]
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[[Category: virus/viral protein]]
[[Category: virus/viral protein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:59:15 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:45 2008''

Revision as of 15:18, 21 February 2008

File:1oke.gif


1oke, resolution 2.4Å

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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 type 3 with and as ligands. This structure supersedes the now removed PDB entry 1OAM. Known structural/functional Site: . 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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