1oke

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{{STRUCTURE_1oke| PDB=1oke | SCENE= }}
{{STRUCTURE_1oke| PDB=1oke | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN IN COMPLEX WITH N-OCTYL-BETA-D-GLUCOSIDE'''
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===CRYSTAL STRUCTURE OF THE DENGUE 2 VIRUS ENVELOPE PROTEIN IN COMPLEX WITH N-OCTYL-BETA-D-GLUCOSIDE===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 12759475 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12759475}}
==About this Structure==
==About this Structure==
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[[Category: Trimer]]
[[Category: Trimer]]
[[Category: Virus/viral protein]]
[[Category: Virus/viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:57:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:19:56 2008''

Revision as of 08:20, 28 July 2008

Template:STRUCTURE 1oke

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

Template:ABSTRACT PUBMED 12759475

About 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.

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 Mon Jul 28 11:19:56 2008

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