The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution.
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.
Rey
F A
FA
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Heinz
F X
FX
Mandl
C
C
Kunz
C
C
Harrison
S C
SC
D000595:Amino Acid Sequence; D000956:Antigens, Viral / Q000737:chemistry; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D004669:Encephalitis Viruses, Tick-Borne / Q000737:chemistry* / Q000472:pathogenicity; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D014759:Viral Envelope Proteins / Q000737:chemistry*; D014774:Virulence
D000956:Antigens, Viral; D014759:Viral Envelope Proteins; C065696:glycoprotein E, Flavivirus