7XWX

Crystal structure of SARS-CoV-2 N-CTD

7XWX の概要

• エントリーDOI: 10.2210/pdb7xwx/pdb
• 分子名称: Nucleoprotein, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: structural protein, drug target, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 89920.60

構造登録者

Luan, X.D.,Li, X.M.,Li, Y.F. (登録日: 2022-05-27, 公開日: 2023-02-08, 最終更新日: 2023-11-29)

主引用文献

Luan, X.,Li, X.,Li, Y.,Su, G.,Yin, W.,Jiang, Y.,Xu, N.,Wang, F.,Cheng, W.,Jin, Y.,Zhang, L.,Xu, H.E.,Xue, Y.,Zhang, S.
Antiviral drug design based on structural insights into the N-terminal domain and C-terminal domain of the SARS-CoV-2 nucleocapsid protein.
Sci Bull (Beijing), 67:2327-2335, 2022

PubMed Abstract: Nucleocapsid (N) protein plays crucial roles in the life cycle of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), including the formation of ribonucleoprotein (RNP) complex with the viral RNA. Here we reported the crystal structures of the N-terminal domain (NTD) and C-terminal domain (CTD) of the N protein and an NTD-RNA complex. Our structures reveal a unique tetramer organization of NTD and identify a distinct RNA binding mode in the NTD-RNA complex, which could contribute to the formation of the RNP complex. We also screened small molecule inhibitors of N-NTD and N-CTD and discovered that ceftriaxone sodium, an antibiotic, can block the binding of RNA to NTD and inhibit the formation of the RNP complex. These results together could facilitate the further research of antiviral drug design targeting N protein.

PubMed: 36317101
DOI: 10.1016/j.scib.2022.10.021

実験手法

X-RAY DIFFRACTION (3 Å)