Publication Abstract from PubMed
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.
The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution.,Rey FA, Heinz FX, Mandl C, Kunz C, Harrison SC Nature. 1995 May 25;375(6529):291-8. PMID:7753193[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
