5tmh
Structure of Zika virus NS5Structure of Zika virus NS5
Structural highlights
Publication Abstract from PubMedThe recent outbreak of Zika virus (ZIKV) has imposed a serious threat to public health. Here we report the crystal structure of the ZIKV NS5 protein in complex with S-adenosyl-L-homocysteine, in which the tandem methyltransferase (MTase) and RNA-dependent RNA polymerase (RdRp) domains stack into one of the two alternative conformations of flavivirus NS5 proteins. The activity of this NS5 protein is verified through a de novo RdRp assay on a subgenomic ZIKV RNA template. Importantly, our structural analysis leads to the identification of a potential drug-binding site of ZIKV NS5, which might facilitate the development of novel antivirals for ZIKV. The structure of Zika virus NS5 reveals a conserved domain conformation.,Wang B, Tan XF, Thurmond S, Zhang ZM, Lin A, Hai R, Song J Nat Commun. 2017 Mar 27;8:14763. doi: 10.1038/ncomms14763. PMID:28345600[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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