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7CE0

Crystal structure of 2019-nCoV nucleocapsid C-terminal domain (CTD) protein

7CE0 の概要
エントリーDOI10.2210/pdb7ce0/pdb
分子名称Nucleoprotein (2 entities in total)
機能のキーワードcovid-19, rna binding, nucleocapsid, 2019-ncov, dimerization, viral protein
由来する生物種Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
タンパク質・核酸の鎖数4
化学式量合計53199.70
構造登録者
Peng, Y.,Qi, J.,Song, H.,Gao, G.F. (登録日: 2020-06-21, 公開日: 2020-09-02, 最終更新日: 2023-11-29)
主引用文献Peng, Y.,Du, N.,Lei, Y.,Dorje, S.,Qi, J.,Luo, T.,Gao, G.F.,Song, H.
Structures of the SARS-CoV-2 nucleocapsid and their perspectives for drug design.
Embo J., 39:e105938-e105938, 2020
Cited by
PubMed Abstract: COVID-19, caused by SARS-CoV-2, has resulted in severe and unprecedented economic and social disruptions in the world. Nucleocapsid (N) protein, which is the major structural component of the virion and is involved in viral replication, assembly and immune regulation, plays key roles in the viral life cycle. Here, we solved the crystal structures of the N- and C-terminal domains (N-NTD and N-CTD) of SARS-CoV-2 N protein, at 1.8 and 1.5 Å resolution, respectively. Both structures show conserved features from other CoV N proteins. The binding sites targeted by small molecules against HCoV-OC43 and MERS-CoV, which inhibit viral infection by blocking the RNA-binding activity or normal oligomerization of N protein, are relatively conserved in our structure, indicating N protein is a promising drug target. In addition, certain areas of N-NTD and N-CTD display distinct charge distribution patterns in SARS-CoV-2, which may alter the RNA-binding modes. The specific antigenic characteristics are critical for developing specific immune-based rapid diagnostic tests. Our structural information can aid in the discovery and development of antiviral inhibitors against SARS-CoV-2 in the future.
PubMed: 32914439
DOI: 10.15252/embj.2020105938
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.5 Å)
構造検証レポート
Validation report summary of 7ce0
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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