2i69
From Proteopedia
Crystal structure of the West Nile virus envelope glycoprotein
Overview
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.
About this Structure
2I69 is a Single protein structure of sequence from West nile virus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 07:07:35 2008
