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From Proteopedia
Crystal structure of SARS-CoV-2 N-NTD and dsRNA complex
Structural highlights
FunctionNCAP_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 PubMedNucleocapsid (N) protein plays crucial roles in the life cycle of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), including the formation of ribonucleoprotein (RNP) complex with the viral RNA. Here we reported the crystal structures of the N-terminal domain (NTD) and C-terminal domain (CTD) of the N protein and an NTD-RNA complex. Our structures reveal a unique tetramer organization of NTD and identify a distinct RNA binding mode in the NTD-RNA complex, which could contribute to the formation of the RNP complex. We also screened small molecule inhibitors of N-NTD and N-CTD and discovered that ceftriaxone sodium, an antibiotic, can block the binding of RNA to NTD and inhibit the formation of the RNP complex. These results together could facilitate the further research of antiviral drug design targeting N protein. Antiviral drug design based on structural insights into the N-terminal domain and C-terminal domain of the SARS-CoV-2 nucleocapsid protein.,Luan X, Li X, Li Y, Su G, Yin W, Jiang Y, Xu N, Wang F, Cheng W, Jin Y, Zhang L, Xu HE, Xue Y, Zhang S Sci Bull (Beijing). 2022 Nov 30;67(22):2327-2335. doi: , 10.1016/j.scib.2022.10.021. Epub 2022 Oct 27. PMID:36317101[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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