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10.1007/s12104-020-09971-6

http://scihub22266oqcxt.onion/10.1007/s12104-020-09971-6
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C7414254!7414254!32770392
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suck abstract from ncbi


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pmid32770392      Biomol+NMR+Assign 2020 ; 14 (2): 329-33
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  • 1H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e #MMPMID32770392
  • Korn SM; Dhamotharan K; Fürtig B; Hengesbach M; Löhr F; Qureshi NS; Richter C; Saxena K; Schwalbe H; Tants JN; Weigand JE; Wöhnert J; Schlundt A
  • Biomol NMR Assign 2020[]; 14 (2): 329-33 PMID32770392show ga
  • The ongoing pandemic caused by the Betacoronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus-2) demonstrates the urgent need of coordinated and rapid research towards inhibitors of the COVID-19 lung disease. The covid19-nmr consortium seeks to support drug development by providing publicly accessible NMR data on the viral RNA elements and proteins. The SARS-CoV-2 genome encodes for approximately 30 proteins, among them are the 16 so-called non-structural proteins (Nsps) of the replication/transcription complex. The 217-kDa large Nsp3 spans one polypeptide chain, but comprises multiple independent, yet functionally related domains including the viral papain-like protease. The Nsp3e sub-moiety contains a putative nucleic acid-binding domain (NAB) with so far unknown function and consensus target sequences, which are conceived to be both viral and host RNAs and DNAs, as well as protein-protein interactions. Its NMR-suitable size renders it an attractive object to study, both for understanding the SARS-CoV-2 architecture and drugability besides the classical virus? proteases. We here report the near-complete NMR backbone chemical shifts of the putative Nsp3e NAB that reveal the secondary structure and compactness of the domain, and provide a basis for NMR-based investigations towards understanding and interfering with RNA- and small-molecule-binding by Nsp3e.
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