1oan

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==Overview==
==Overview==
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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.
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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==
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[[Category: Dengue virus type 3]]
[[Category: Dengue virus type 3]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Harrison, S.C.]]
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[[Category: Harrison, S C.]]
[[Category: Modis, Y.]]
[[Category: Modis, Y.]]
[[Category: NA]]
[[Category: NA]]
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[[Category: membrane fusion]]
[[Category: membrane fusion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:55:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:25 2008''

Revision as of 12:15, 21 February 2008


1oan, resolution 2.75Å

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CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN

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

1OAN is a Single protein structure of sequence from Dengue virus type 3 with and as ligands. 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

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