The envelope glycoprotein from tick-borne encephalitis virus at 2 Å 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...

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Bibliographic Details
Published in:Nature (London) 1995-05, Vol.375 (6529), p.291-298
Main Authors: Rey, Félix A., Heinz, Franz X., Mandl, Christian, Kunz, Christian, Harrison, Stephen C.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antigens, Viral - chemistry
Biological and medical sciences
Computer Graphics
Crystallography, X-Ray
Encephalitis Viruses, Tick-Borne - chemistry
Encephalitis Viruses, Tick-Borne - pathogenicity
Fundamental and applied biological sciences. Psychology
Humanities and Social Sciences
Hydrogen-Ion Concentration
Microbiology
Molecular Sequence Data
Morphology, structure, chemical composition, physicochemical properties
multidisciplinary
Protein Conformation
Science
Science (multidisciplinary)
Sequence Homology, Amino Acid
Viral Envelope Proteins - chemistry
Virology
Virulence
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/375291a0