6M3M
Crystal structure of SARS-CoV-2 nucleocapsid protein N-terminal RNA binding domain
Summary for 6M3M
Entry DOI | 10.2210/pdb6m3m/pdb |
Descriptor | Nucleoprotein (2 entities in total) |
Functional Keywords | coronavirus, nucleocapsid protein, rna binding domain, sars-cov 2, ntd, viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
Total number of polymer chains | 4 |
Total formula weight | 59578.36 |
Authors | |
Primary citation | Kang, S.,Yang, M.,Hong, Z.,Zhang, L.,Huang, Z.,Chen, X.,He, S.,Zhou, Z.,Zhou, Z.,Chen, Q.,Yan, Y.,Zhang, C.,Shan, H.,Chen, S. Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites. Acta Pharm Sin B, 10:1228-1238, 2020 Cited by PubMed Abstract: The outbreak of coronavirus disease (COVID-19) caused by SARS-CoV-2 virus continually lead to worldwide human infections and deaths. Currently, there is no specific viral protein-targeted therapeutics. Viral nucleocapsid protein is a potential antiviral drug target, serving multiple critical functions during the viral life cycle. However, the structural information of SARS-CoV-2 nucleocapsid protein remains unclear. Herein, we have determined the 2.7 Å crystal structure of the N-terminal RNA binding domain of SARS-CoV-2 nucleocapsid protein. Although the overall structure is similar as other reported coronavirus nucleocapsid protein N-terminal domain, the surface electrostatic potential characteristics between them are distinct. Further comparison with mild virus type HCoV-OC43 equivalent domain demonstrates a unique potential RNA binding pocket alongside the -sheet core. Complemented by binding studies, our data provide several atomic resolution features of SARS-CoV-2 nucleocapsid protein N-terminal domain, guiding the design of novel antiviral agents specific targeting to SARS-CoV-2. PubMed: 32363136DOI: 10.1016/j.apsb.2020.04.009 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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