Structural highlights
Function
A0A109PRQ3_ZIKV Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504] Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859]
Publication Abstract from PubMed
Zika virus (ZIKV) has emerged as major health concern, as ZIKV infection has been shown to be associated with microcephaly, severe neurological disease and possibly male sterility. As the largest protein component within the ZIKV replication complex, NS5 plays key roles in the life cycle and survival of the virus through its N-terminal methyltransferase (MTase) and C-terminal RNA-dependent RNA polymerase (RdRp) domains. Here, we present the crystal structures of ZIKV NS5 MTase in complex with an RNA cap analogue (m7GpppA) and the free NS5 RdRp. We have identified the conserved features of ZIKV NS5 MTase and RdRp structures that could lead to development of current antiviral inhibitors being used against flaviviruses, including dengue virus and West Nile virus, to treat ZIKV infection. These results should inform and accelerate the structure-based design of antiviral compounds against ZIKV.
The crystal structure of Zika virus NS5 reveals conserved drug targets.,Duan W, Song H, Wang H, Chai Y, Su C, Qi J, Shi Y, Gao GF EMBO J. 2017 Apr 3;36(7):919-933. doi: 10.15252/embj.201696241. Epub 2017 Mar 2. PMID:28254839[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Duan W, Song H, Wang H, Chai Y, Su C, Qi J, Shi Y, Gao GF. The crystal structure of Zika virus NS5 reveals conserved drug targets. EMBO J. 2017 Apr 3;36(7):919-933. doi: 10.15252/embj.201696241. Epub 2017 Mar 2. PMID:28254839 doi:http://dx.doi.org/10.15252/embj.201696241
