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10.1007/s12104-020-10000-9

http://scihub22266oqcxt.onion/10.1007/s12104-020-10000-9
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suck abstract from ncbi


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pmid33423172      Biomol+NMR+Assign 2021 ; 15 (1): 165-171
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  • (1)H,(13)C and (15)N chemical shift assignments of the SUD domains of SARS-CoV-2 non-structural protein 3c: "The SUD-M and SUD-C domains" #MMPMID33423172
  • Gallo A; Tsika AC; Fourkiotis NK; Cantini F; Banci L; Sreeramulu S; Schwalbe H; Spyroulias GA
  • Biomol NMR Assign 2021[Apr]; 15 (1): 165-171 PMID33423172show ga
  • SARS-CoV-2 RNA, nsP3c (non-structural Protein3c) spans the sequence of the so-called SARS Unique Domains (SUDs), first observed in SARS-CoV. Although the function of this viral protein is not fully elucidated, it is believed that it is crucial for the formation of the replication/transcription viral complex (RTC) and of the interaction of various viral "components" with the host cell; thus, it is essential for the entire viral life cycle. The first two SUDs, the so-called SUD-N (the N-terminal domain) and SUD-M (domain following SUD-N) domains, exhibit topological and conformational features that resemble the nsP3b macro (or "X") domain. Indeed, they are all folded in a three-layer alpha/beta/alpha sandwich structure, as revealed through crystallographic structural investigation of SARS-CoV SUDs, and they have been attributed to different substrate selectivity as they selectively bind to oligonucleotides. On the other hand, the C-terminal SUD (SUD-C) exhibit much lower sequence similarities compared to the SUD-N & SUD-M, as reported in previous crystallographic and NMR studies of SARS-CoV. In the absence of the 3D structures of SARS-CoV-2, we report herein the almost complete NMR backbone and side-chain resonance assignment ((1)H,(13)C,(15)N) of SARS-CoV-2 SUD-M and SUD-C proteins, and the NMR chemical shift-based prediction of their secondary structure elements. These NMR data will set the base for further understanding at the atomic-level conformational dynamics of these proteins and will allow the effective screening of a large number of small molecules as binders with potential biological impact on their function.
  • |*Magnetic Resonance Spectroscopy[MESH]
  • |Carbon Isotopes[MESH]
  • |Coronavirus Papain-Like Proteases/*chemistry[MESH]
  • |Hydrogen[MESH]
  • |Nitrogen Isotopes[MESH]
  • |Protein Binding[MESH]
  • |Protein Domains[MESH]
  • |Protein Structure, Secondary[MESH]


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