5WZ1

Crystal structure of Zika virus NS5 methyltransferase bound to S-adenosyl-L-methionine

5WZ1 の概要

• エントリーDOI: 10.2210/pdb5wz1/pdb
• 関連するPDBエントリー: 5WZ2 5WZ3
• 分子名称: NS5 methyltransferase, S-ADENOSYLMETHIONINE (2 entities in total)
• 機能のキーワード: zika virus, methyltransferase, mtase, sam, transferase
• 由来する生物種: Zika virus (strain Mr 766) (ZIKV)
• 細胞内の位置: Virion membrane ; Multi-pass membrane protein : A0A140E7U5
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 248715.53

構造登録者

Duan, W.,Song, H.,Qi, J.,Shi, Y.,Gao, G.F. (登録日: 2017-01-16, 公開日: 2017-03-08, 最終更新日: 2023-11-22)

主引用文献

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

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: 28254839
DOI: 10.15252/embj.201696241

実験手法

X-RAY DIFFRACTION (2.507 Å)