7F2E
SARS-CoV-2 nucleocapsid protein C-terminal domain (dodecamer)
7F2E の概要
| エントリーDOI | 10.2210/pdb7f2e/pdb |
| 分子名称 | Nucleoprotein, PHOSPHATE ION (3 entities in total) |
| 機能のキーワード | sars-cov-2 nucleocapsid protein, viral protein |
| 由来する生物種 | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 147100.93 |
| 構造登録者 | |
| 主引用文献 | Jia, Z.,Liu, C.,Chen, Y.,Jiang, H.,Wang, Z.,Yao, J.,Yang, J.,Zhu, J.,Zhang, B.,Yuchi, Z. Crystal structures of the SARS-CoV-2 nucleocapsid protein C-terminal domain and development of nucleocapsid-targeting nanobodies. Febs J., 289:3813-3825, 2022 Cited by PubMed Abstract: The ongoing outbreak of COVID-19 caused by SARS-CoV-2 has resulted in a serious public health threat globally. Nucleocapsid protein is a major structural protein of SARS-CoV-2 that plays important roles in the viral RNA packing, replication, assembly, and infection. Here, we report two crystal structures of nucleocapsid protein C-terminal domain (CTD) at resolutions of 2.0 Å and 3.1 Å, respectively. These two structures, crystallized under different conditions, contain 2 and 12 CTDs in asymmetric unit, respectively. Interestingly, despite different crystal packing, both structures show a similar dimeric form as the smallest unit, consistent with its solution form measured by the size-exclusion chromatography, suggesting an important role of CTD in the dimerization of nucleocapsid proteins. By analyzing the surface charge distribution, we identified a stretch of positively charged residues between Lys257 and Arg262 that are involved in RNA-binding. Through screening a single-domain antibodies (sdAbs) library, we identified four sdAbs targeting different regions of nucleocapsid protein with high affinities that have future potential to be used in viral detection and therapeutic purposes. PubMed: 34665939DOI: 10.1111/febs.16239 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.1 Å) |
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