7c22
From Proteopedia
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== Function == | == Function == | ||
[[https://www.uniprot.org/uniprot/NCAP_SARS2 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. | [[https://www.uniprot.org/uniprot/NCAP_SARS2 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The newly emerging severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in a global human health crisis. The CoV nucleocapsid (N) protein plays essential roles both in the viral genomic RNA packaging and the regulation of host cellular machinery. Here, to contribute to the structural information of the N protein, we describe the 2.0 A crystal structure of the SARS-CoV-2 N protein C-terminal domain (N-CTD). The structure indicates an extensive interaction dimer in a domain-swapped manner. The interface of this dimer was first thoroughly illustrated. Also, the SARS-CoV-2 N-CTD dimerization form was verified in solution using size-exclusion chromatography. Based on the structural comparison of the N-CTDs from alpha-, beta-, and gamma-CoVs, we demonstrate the common and specific characteristics of the SARS-CoV-2 N-CTD. Furthermore, we provide evidence that the SARS-CoV-2 N-CTD possesses the binding ability to single-stranded RNA, single-stranded DNA as well as double-stranded DNA in vitro. In conclusion, this study could potentially accelerate research to understand the complete biological functions of the new CoV N protein. | ||
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| + | Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein.,Zhou R, Zeng R, von Brunn A, Lei J Mol Biomed. 2020 Aug 6;1(1):2. doi: 10.1186/s43556-020-00001-4. PMID:35006385<ref>PMID:35006385</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7c22" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]] | *[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:47, 16 February 2022
Crystal structure of the C-terminal domain of SARS-CoV-2 nucleocapsid protein
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Categories: 2019-ncov | Large Structures | Lei, J | Zeng, R | Zhou, R J | Coronavirus | Dimerization | Nucleocapsid | Sars-cov-2 | Viral protein
