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Due to its central role in RNA viral replication, the non-structural protein 5 (NS5) RNA-dependent RNA-polymerase (RdRp) is a prime target for drug discovery. Here we describe the crystal structure of the recombinant ZIKV NS5 RdRp domain at 1.9\u2009\u00c5 resolution as a platform for structure-based drug design strategy. The overall structure is similar to other flaviviral homologues. However, the priming loop target site, which is suitable for non-nucleoside polymerase inhibitor design, shows significant differences in comparison with the dengue virus structures, including a tighter pocket and a modified local charge distribution.<\/jats:p>","DOI":"10.1038\/ncomms14764","type":"journal-article","created":{"date-parts":[[2017,3,27]],"date-time":"2017-03-27T05:33:53Z","timestamp":1490592833000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":117,"title":["Crystal structure of Zika virus NS5 RNA-dependent RNA polymerase"],"prefix":"10.1038","volume":"8","author":[{"given":"Andre S.","family":"Godoy","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gustavo M. A.","family":"Lima","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ketllyn I. 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