7CE0

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

Summary for 7CE0

• Entry DOI: 10.2210/pdb7ce0/pdb
• Descriptor: Nucleoprotein (2 entities in total)
• Functional Keywords: covid-19, rna binding, nucleocapsid, 2019-ncov, dimerization, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• Total number of polymer chains: 4
• Total formula weight: 53199.70

Authors

Peng, Y.,Qi, J.,Song, H.,Gao, G.F. (deposition date: 2020-06-21, release date: 2020-09-02, Last modification date: 2023-11-29)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)