About: (1)H, (13)C, and (15)N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e

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About: (1)H, (13)C, and (15)N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	(1)H, (13)C, and (15)N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e
Creator	Wöhnert, Jens Saxena, Krishna Schwalbe, Harald Fürtig, Boris Löhr, · Dhamotharan, Karthikeyan Hengesbach, Martin Korn, Sophie Qureshi, Nusrat Richter, Christian Schlundt, Andreas Tants, Jan-Niklas Weigand, Julia
Source	Medline; PMC
abstract	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.
has issue date	2020-08-08(xsd:dateTime)
bibo:doi	10.1007/s12104-020-09971-6
bibo:pmid	32770392
has license	cc-by
sha1sum (hex)	647f671afa4b3a3a1c690246740e85fd66009992
schema:url	https://doi.org/10.1007/s12104-020-09971-6
resource representing a document's title	(1)H, (13)C, and (15)N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e
has PubMed Central identifier	PMC7414254
has PubMed identifier	32770392
schema:publication	Biomol NMR Assign
resource representing a document's body	covid:647f671afa4b3a3a1c690246740e85fd66009992#body_text
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