Structural highlights
Function[NCAP_SARS2] Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Publication Abstract from PubMedThe 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 (1)H-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. Atomic-Resolution Structure of SARS-CoV-2 Nucleocapsid Protein N-Terminal Domain.,Sarkar S, Runge B, Russell RW, Movellan KT, Calero D, Zeinalilathori S, Quinn CM, Lu M, Calero G, Gronenborn AM, Polenova T J Am Chem Soc. 2022 May 31. doi: 10.1021/jacs.2c03320. PMID:35638584[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 05:21, 15 June 2022.