2i69

Crystal structure of the West Nile virus envelope glycoprotein

spinqualitylabelsall models 2i69, resolution 3.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2i69 is a 1 chain structure with sequence from Wnv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FUL, NAG Gene: Envelope protein (WNV) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed West Nile virus, a member of the Flavivirus genus, causes fever that can progress to life-threatening encephalitis. The major envelope glycoprotein, E, of these viruses mediates viral attachment and entry by membrane fusion. We have determined the crystal structure of a soluble fragment of West Nile virus E. The structure adopts the same overall fold as that of the E proteins from dengue and tick-borne encephalitis viruses. The conformation of domain II is different from that in other prefusion E structures, however, and resembles the conformation of domain II in postfusion E structures. The epitopes of neutralizing West Nile virus-specific antibodies map to a region of domain III that is exposed on the viral surface and has been implicated in receptor binding. In contrast, we show that certain recombinant therapeutic antibodies, which cross-neutralize West Nile and dengue viruses, bind a peptide from domain I that is exposed only during the membrane fusion transition. By revealing the details of the molecular landscape of the West Nile virus surface, our structure will assist the design of antiviral vaccines and therapeutics. Crystal structure of west nile virus envelope glycoprotein reveals viral surface epitopes.,Kanai R, Kar K, Anthony K, Gould LH, Ledizet M, Fikrig E, Marasco WA, Koski RA, Modis Y J Virol. 2006 Nov;80(22):11000-8. Epub 2006 Aug 30. PMID:16943291 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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