Download MendeleyThe envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution.
Rey, F.A., Heinz, F.X., Mandl, C., Kunz, C., Harrison, S.C.(1995) Nature 375: 291-298
- PubMed: 7753193
- DOI: https://doi.org/10.1038/375291a0
- Primary Citation of Related Structures:
1SVB - PubMed Abstract:
The crystallographically determined structure of a soluble fragment from the major envelope protein of a flavivirus reveals an unusual architecture. The flat, elongated dimer extends in a direction that would be parallel to the viral membrane. Residues that influence binding of monoclonal antibodies lie on the outward-facing surface of the protein. The clustering of mutations that affect virulence in various flaviviruses indicates a possible receptor binding site and, together with other mutational and biochemical data, suggests a picture for the fusion-activating, conformational change triggered by low pH.
Organizational Affiliation:
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
