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10.1007/s12104-020-09998-9

http://scihub22266oqcxt.onion/10.1007/s12104-020-09998-9
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suck abstract from ncbi


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pmid33389548      Biomol+NMR+Assign 2021 ; 15 (1): 153-157
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  • (1)H, (15)N and (13)C resonance assignments of the N-terminal domain of the nucleocapsid protein from the endemic human coronavirus HKU1 #MMPMID33389548
  • de Luna Marques A; Caruso IP; Santana-Silva MC; Bezerra PR; Araujo GR; Almeida FCL; Amorim GC
  • Biomol NMR Assign 2021[Apr]; 15 (1): 153-157 PMID33389548show ga
  • Coronaviruses have become of great medical and scientific interest because of the Covid-19 pandemic. The hCoV-HKU1 is an endemic betacoronavirus that causes mild respiratory symptoms, although the infection can progress to severe lung disease and death. During viral replication, a discontinuous transcription of the genome takes place, producing the subgenomic messenger RNAs. The nucleocapsid protein (N) plays a pivotal role in the regulation of this process, acting as an RNA chaperone and participating in the nucleocapsid assembly. The isolated N-terminal domain of protein N (N-NTD) specifically binds to the transcriptional regulatory sequences and control the melting of the double-stranded RNA. Here, we report the resonance assignments of the N-NTD of HKU1-CoV.
  • |*Magnetic Resonance Spectroscopy[MESH]
  • |Betacoronavirus/*chemistry[MESH]
  • |Carbon Isotopes[MESH]
  • |Coronavirus Nucleocapsid Proteins/*chemistry[MESH]
  • |Escherichia coli/metabolism[MESH]
  • |Hydrogen[MESH]
  • |Nitrogen Isotopes[MESH]
  • |Protein Binding[MESH]
  • |Protein Domains[MESH]
  • |Protein Structure, Secondary[MESH]


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