Abstract
The envelope (E) protein of flaviviruses is an attractive target for the development of antiviral agents because this protein plays an important role in the formation of virus particles and in the virus invasion in host cells. Currently, there is no specific antiviral therapy for tick-borne encephalitis. The goal of this study is to determine the crystal structure of the envelope (E) protein ectodomain of Far-Eastern tick-borne encephalitis virus subtype (Sofjin strain). The knowledge of the three-dimensional structure can serve as the basis for the development of specific inhibitors of conformational rearrangements of the (E) protein, which are essential for the initial stages of infection.
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