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The Zika virus belongs to the family Flaviridae and is known to cause Zika Fever. The ZF was related to the increase in cases of microcephaly in newborns whose mothers had infections during pregnancy. The major protein of ZIKV is the NS5 protein, it has two domains, a methyltransferase and another RNA-dependent RNA polymerase (RdRp), responsible for RNA-polymerization, both domains are necessary for viral RNA replication. In this context, our objective is to elucidate the crystallographic structure of RdRp domain, find ligands and putative inhibitors. After setting this goal, the structure for RdRp was elucidated by our group.1 After that, we performed the screening of fragments and compounds, from a library provided by Prof. Dr. Marcio Dias (ICB/USP). Biophysical assays2,3 are being performed to search for ligands, which provided some promising hits, which are now being submitted to inhibition assays and analysis of their possible interaction with the structure.
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