The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution

Nature. 1995 May 25;375(6529):291-8. doi: 10.1038/375291a0.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antigens, Viral / chemistry
  • Computer Graphics
  • Crystallography, X-Ray
  • Encephalitis Viruses, Tick-Borne / chemistry*
  • Encephalitis Viruses, Tick-Borne / pathogenicity
  • Hydrogen-Ion Concentration
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Viral Envelope Proteins / chemistry*
  • Virulence


  • Antigens, Viral
  • Viral Envelope Proteins
  • glycoprotein E, Flavivirus