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Nature. 1995 May 25;375(6529):291-8.

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

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  • 1Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.

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.

PMID:
7753193
DOI:
10.1038/375291a0
[PubMed - indexed for MEDLINE]
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