5WZ3
Crystal structure of Zika virus NS5 RNA-dependent RNA polymerase(RdRP)
Summary for 5WZ3
| Entry DOI | 10.2210/pdb5wz3/pdb |
| Related | 5WZ1 5WZ2 |
| Descriptor | NS5 RdRp, ZINC ION (3 entities in total) |
| Functional Keywords | zika virus, ns5, rdrp, rna-dependent rna polymerase, transferase |
| Biological source | Zika virus (ZIKV) |
| Cellular location | Virion membrane ; Multi-pass membrane protein : A0A1B2ZC85 |
| Total number of polymer chains | 1 |
| Total formula weight | 72205.86 |
| Authors | |
| Primary citation | Duan, W.,Song, H.,Wang, H.,Chai, Y.,Su, C.,Qi, J.,Shi, Y.,Gao, G.F. The crystal structure of Zika virus NS5 reveals conserved drug targets. EMBO J., 36:919-933, 2017 Cited by PubMed Abstract: 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 (GpppA) 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. PubMed: 28254839DOI: 10.15252/embj.201696241 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.804 Å) |
Structure validation
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