Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 144, Issue 23, Pages 10543-10555Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.2c03320
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Funding
- National Institutes of Health (NIH) [P50AI1504817, P30GM133894]
- National Institu tes of Heal th (NIGMS) [P30GM110758]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
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This study determined the atomic-resolution structure of the N-terminal domain (N-NTD) of the nucleocapsid (N) protein of the SARS-CoV-2 virus using solid-state magic angle spinning (MAS) NMR and X-ray diffraction techniques. The structure provides information about protein packing interfaces, flexible regions, and the functionally important RNA binding. It offers guidance for designing therapeutic interventions against SARS-CoV-2 infection.
The nucleocapsid (N) protein is one of the four structural proteins of the SARS-CoV-2 virus and plays a crucial role in viral genome organization and, hence, replication and pathogenicity. The N-terminal domain (N-NTD) binds to the genomic RNA and thus comprises a potential target for inhibitor and vaccine development. We determined the atomic-resolution structure of crystalline N-NTD by integrating solid-state magic angle spinning (MAS) NMR and X-ray diffraction. Our combined approach provides atomic details of protein packing interfaces as well as information about flexible regions as the N- and C-termini and the functionally important RNA binding, beta-hairpin loop. In addition, ultrafast (100 kHz) MAS H-1-detected experiments permitted the assignment of side-chain proton chemical shifts not available by other means. The present structure offers guidance for designing therapeutic interventions against the SARS-CoV-2 infection.
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