Crystal structure of the dengue 2 virus envelope glycoprotein in the postfusion conformationCrystal structure of the dengue 2 virus envelope glycoprotein in the postfusion conformation

Structural highlights

1ok8 is a 1 chain structure with sequence from Dengue virus 2. The July 2008 RCSB PDB Molecule of the Month feature on Dengue Virus by David Goodsell is 10.2210/rcsb_pdb/mom_2008_7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

Dengue virus enters a host cell when the viral envelope glycoprotein, E, binds to a receptor and responds by conformational rearrangement to the reduced pH of an endosome. The conformational change induces fusion of viral and host-cell membranes. A three-dimensional structure of the soluble E ectodomain (sE) in its trimeric, postfusion state reveals striking differences from the dimeric, prefusion form. The elongated trimer bears three 'fusion loops' at one end, to insert into the host-cell membrane. Their structure allows us to model directly how these fusion loops interact with a lipid bilayer. The protein folds back on itself, directing its carboxy terminus towards the fusion loops. We propose a fusion mechanism driven by essentially irreversible conformational changes in E and facilitated by fusion-loop insertion into the outer bilayer leaflet. Specific features of the folded-back structure suggest strategies for inhibiting flavivirus entry.

Structure of the dengue virus envelope protein after membrane fusion.,Modis Y, Ogata S, Clements D, Harrison SC Nature. 2004 Jan 22;427(6972):313-9. PMID:14737159[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Modis Y, Ogata S, Clements D, Harrison SC. Structure of the dengue virus envelope protein after membrane fusion. Nature. 2004 Jan 22;427(6972):313-9. PMID:14737159 doi:10.1038/nature02165

1ok8, resolution 2.00Å

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