作者
Andre S Godoy, Gustavo MA Lima, Ketllyn IZ Oliveira, Naiara U Torres, Fernando V Maluf, Rafael VC Guido, Glaucius Oliva
发表日期
2017/3/27
期刊
Nature communications
卷号
8
期号
1
页码范围
14764
出版商
Nature Publishing Group UK
简介
The current Zika virus (ZIKV) outbreak became a global health threat of complex epidemiology and devastating neurological impacts, therefore requiring urgent efforts towards the development of novel efficacious and safe antiviral drugs. 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 Å 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.
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AS Godoy, GMA Lima, KIZ Oliveira, NU Torres… - Nature communications, 2017