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The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution | | F A Rey
; F X Heinz
; C Mandl
; C Kunz
; S C Harrison
; | | Date: |
25 May 1995 | | Journal: | Nature, 375 (6529), 291-8 | | 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. | | Source: | PubMed, pmid7753193 doi: 10.1038/375291a0 | | Services: | Forum | Review | Favorites | |
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