5KQR

Structure of NS5 methyltransferase from Zika virus bound to S-adenosylmethionine

5KQR の概要

• エントリーDOI: 10.2210/pdb5kqr/pdb
• 分子名称: Methyltransferase, S-ADENOSYLMETHIONINE, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: zika, flavivirus, transferase
• 由来する生物種: Zika virus (ZIKV)
• 細胞内の位置: Virion membrane ; Multi-pass membrane protein : H9A910
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30067.60

構造登録者

Jain, R.,Coloma, J.,Rajashankar, K.R.,Aggarwal, A.K. (登録日: 2016-07-06, 公開日: 2016-09-14, 最終更新日: 2023-10-04)

主引用文献

Coloma, J.,Jain, R.,Rajashankar, K.R.,Garcia-Sastre, A.,Aggarwal, A.K.
Structures of NS5 Methyltransferase from Zika Virus.
Cell Rep, 16:3097-3102, 2016

PubMed Abstract: The Zika virus (ZIKV) poses a major public health emergency. To aid in the development of antivirals, we present two high-resolution crystal structures of the ZIKV NS5 methyltransferase: one bound to S-adenosylmethionine (SAM) and the other bound to SAM and 7-methyl guanosine diphosphate (7-MeGpp). We identify features of ZIKV NS5 methyltransferase that lend to structure-based antiviral drug discovery. Specifically, SAM analogs with functionalities on the Cβ atom of the methionine portion of the molecules that occupy the RNA binding tunnel may provide better specificity relative to human RNA methyltransferases.

PubMed: 27633330
DOI: 10.1016/j.celrep.2016.08.091

実験手法

X-RAY DIFFRACTION (1.331 Å)