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1oke
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Dengue virus is an emerging global health threat. Its major envelope | + | 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 | + | 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 | + | [[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 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:45 2008'' |
Revision as of 12:18, 21 February 2008
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CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN IN COMPLEX WITH N-OCTYL-BETA-D-GLUCOSIDE
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.
About 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.
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:12759475
Page seeded by OCA on Thu Feb 21 14:18:45 2008
