About: (1)H, (13)C, and (15)N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b

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About: (1)H, (13)C, and (15)N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	(1)H, (13)C, and (15)N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b
Creator	Qureshi, · Weigand, · Hutchison, · Altincekic, · Bains, · Banci, · Cantini, F Dhamotharan, · Fourkiotis, · Fuks, · Fürtig, · Gande, · Hargittay, · Hengesbach, · Korn, · Kubatova, · Kutz, · Linhard, · Löhr, · Meiser, · Pyper, · Richter, · Saxena, · Schlundt, · Schwalbe, · Spyroulias, G Sreeramulu, · Tants, J.-N Tsika, · Wacker, · Wöhnert, ·
source	Medline; PMC
abstract	The SARS-CoV-2 genome encodes for approximately 30 proteins. Within the international project COVID19-NMR, we distribute the spectroscopic analysis of the viral proteins and RNA. Here, we report NMR chemical shift assignments for the protein Nsp3b, a domain of Nsp3. The 217-kDa large Nsp3 protein contains multiple structurally independent, yet functionally related domains including the viral papain-like protease and Nsp3b, a macrodomain (MD). In general, the MDs of SARS-CoV and MERS-CoV were suggested to play a key role in viral replication by modulating the immune response of the host. The MDs are structurally conserved. They most likely remove ADP-ribose, a common posttranslational modification, from protein side chains. This de-ADP ribosylating function has potentially evolved to protect the virus from the anti-viral ADP-ribosylation catalyzed by poly-ADP-ribose polymerases (PARPs), which in turn are triggered by pathogen-associated sensing of the host immune system. This renders the SARS-CoV-2 Nsp3b a highly relevant drug target in the viral replication process. We here report the near-complete NMR backbone resonance assignment ((1)H, (13)C, (15)N) of the putative Nsp3b MD in its apo form and in complex with ADP-ribose. Furthermore, we derive the secondary structure of Nsp3b in solution. In addition, (15)N-relaxation data suggest an ordered, rigid core of the MD structure. These data will provide a basis for NMR investigations targeted at obtaining small-molecule inhibitors interfering with the catalytic activity of Nsp3b.
has issue date	2020-08-14(xsd:dateTime)
bibo:doi	10.1007/s12104-020-09973-4
bibo:pmid	32803496
has license	cc-by
sha1sum (hex)	0be3f5104c1ebfff6f6564b74b54d6bf62d86e7c
schema:url	https://doi.org/10.1007/s12104-020-09973-4
resource representing a document's title	(1)H, (13)C, and (15)N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b
has PubMed Central identifier	PMC7428200
has PubMed identifier	32803496
schema:publication	Biomol NMR Assign
resource representing a document's body	covid:0be3f5104c1ebfff6f6564b74b54d6bf62d86e7c#body_text
is schema:about of	named entity 'proteins' named entity 'multiple' named entity 'domains' named entity 'ordered' named entity 'viral' named entity 'protein' named entity 'targeted' named entity 'viral' named entity 'MDs' named entity 'RNA' named entity 'HIGHLY' named entity 'ITS' named entity 'VIRUS' named entity 'ASSIGNMENT' named entity 'SOLUTION' named entity 'PROTEINS' named entity 'ADDITION' named entity 'RELAXATION' named entity 'virus' named entity 'Within' named entity 'domain' named entity 'common' named entity 'genome' named entity 'assignments' named entity 'function' named entity 'encodes' named entity 'catalytic activity' named entity 'MDs' named entity 'viral replication' named entity 'renders' named entity 'NMR' named entity 'ADP-ribosylation' named entity 'papain' named entity 'secondary structure' named entity 'pathogen' named entity 'SARS-CoV-2' named entity 'COVID19' named entity 'poly-ADP-ribose polymerases' named entity 'GenBank' named entity 'X-ray structures' named entity 'innate immune' named entity 'E. coli' named entity 'protease inhibitor' named entity 'secondary structure' named entity 'genomes' named entity 'ADP-ribose' named entity 'TEV' named entity 'NMR spectrometer' named entity 'Bruker' named entity 'protein' named entity 'chemical shift'

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