7CE0
Crystal structure of 2019-nCoV nucleocapsid C-terminal domain (CTD) protein
7CE0 の概要
| エントリーDOI | 10.2210/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 | |
| 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: 32914439DOI: 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) |
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