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

2020 ◽  
Vol 14 (2) ◽  
pp. 339-346 ◽  
Author(s):  
F. Cantini ◽  
L. Banci ◽  
N. Altincekic ◽  
J. K. Bains ◽  
K. Dhamotharan ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Assignments ◽  
Structural Protein ◽  
Backbone Chemical Shift

scholarly journals 1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein)

2021 ◽  
Author(s):  
Ying Wang ◽  
John Kirkpatrick ◽  
Susanne zur Lage ◽  
Sophie M. Korn ◽  
Konstantin Neißner ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Open Reading Frames ◽  
Viral Rna ◽  
Backbone Dynamics ◽  
Chemical Shift Assignments ◽  
Immune Functions ◽  
Structural Protein ◽  
Health Crisis ◽  
Backbone Chemical Shift ◽  
Reading Frames

AbstractThe current COVID-19 pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has become a worldwide health crisis, necessitating coordinated scientific research and urgent identification of new drug targets for treatment of 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 comprises a single RNA of about 30 kb in length, in which 14 open reading frames (ORFs) have been annotated, and encodes approximately 30 proteins. The first two-thirds of the SARS-CoV-2 genome is made up of two large overlapping open-reading-frames (ORF1a and ORF1b) encoding a replicase polyprotein, which is subsequently cleaved to yield 16 so-called non-structural proteins. The non-structural protein 1 (Nsp1), which is considered to be a major virulence factor, suppresses host immune functions by associating with host ribosomal complexes at the very end of its C-terminus. Furthermore, Nsp1 facilitates initiation of viral RNA translation via an interaction of its N-terminal domain with the 5′ untranslated region (UTR) of the viral RNA. Here, we report the near-complete backbone chemical-shift assignments of full-length SARS-CoV-2 Nsp1 (19.8 kDa), which reveal the domain organization, secondary structure and backbone dynamics of Nsp1, and which will be of value to further NMR-based investigations of both the biochemical and physiological functions of Nsp1.

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

2020 ◽  
Vol 14 (2) ◽  
pp. 329-333
Author(s):  
Sophie M. Korn ◽  
Karthikeyan Dhamotharan ◽  
Boris Fürtig ◽  
Martin Hengesbach ◽  
Frank Löhr ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Chemical Shift ◽  
Binding Domain ◽  
Chemical Shift Assignments ◽  
Nucleic Acid Binding ◽  
Structural Protein ◽  
Backbone Chemical Shift

Toho-1 β-lactamase: backbone chemical shift assignments and changes in dynamics upon binding with avibactam

2021 ◽  
Author(s):  
Varun V. Sakhrani ◽  
Rittik K. Ghosh ◽  
Eduardo Hilario ◽  
Kevin L. Weiss ◽  
Leighton Coates ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Assignments ◽  
Backbone Chemical Shift

1H, 13C, and 15N backbone chemical shift assignments of StAR-related lipid transfer domain protein 5 (STARD5)

2012 ◽  
Vol 7 (1) ◽  
pp. 21-24 ◽  
Author(s):  
Aurélien Lorin ◽  
Danny Létourneau ◽  
Andrée Lefebvre ◽  
Jean-Guy LeHoux ◽  
Pierre Lavigne
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Assignments ◽  
Lipid Transfer ◽  
Backbone Chemical Shift ◽  
Domain Protein

scholarly journals Backbone chemical shift assignments of mouse HOXA13 DNA binding domain bound to duplex DNA

2010 ◽  
Vol 4 (1) ◽  
pp. 97-99 ◽  
Author(s):  
Yonghong Zhang ◽  
Chelsea K. Thornburg ◽  
H. Scott Stadler ◽  
James B. Ames
Keyword(s):  
Chemical Shift ◽  
Dna Binding ◽  
Binding Domain ◽  
Duplex Dna ◽  
Dna Binding Domain ◽  
Chemical Shift Assignments ◽  
Backbone Chemical Shift

scholarly journals 1H, 13C, and 15N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7

2020 ◽  
Author(s):  
Marco Tonelli ◽  
Chad Rienstra ◽  
Thomas K. Anderson ◽  
Rob Kirchdoerfer ◽  
Katherine Henzler-Wildman
Keyword(s):  
Chemical Shift ◽  
Side Chain ◽  
Chemical Shift Assignments ◽  
Structural Protein ◽  
Side Chain Chemical Shift

scholarly journals 1H, 13C, and 15N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein

2020 ◽  
Author(s):  
Sophie M. Korn ◽  
Roderick Lambertz ◽  
Boris Fürtig ◽  
Martin Hengesbach ◽  
Frank Löhr ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Nucleocapsid Protein ◽  
Rna Binding ◽  
Drug Binding ◽  
Chemical Shift Assignments ◽  
Binding Studies ◽  
Dimerization Domain ◽  
N Protein ◽  
Intrinsically Disordered ◽  
Backbone Chemical Shift

AbstractThe current outbreak of the highly infectious COVID-19 respiratory disease is caused by the novel coronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2). To fight the pandemic, the search for promising viral drug targets has become a cross-border common goal of the international biomedical research community. Within the international Covid19-NMR consortium, scientists support drug development against SARS-CoV-2 by providing publicly available NMR data on viral proteins and RNAs. The coronavirus nucleocapsid protein (N protein) is an RNA-binding protein involved in viral transcription and replication. Its primary function is the packaging of the viral RNA genome. The highly conserved architecture of the coronavirus N protein consists of an N-terminal RNA-binding domain (NTD), followed by an intrinsically disordered Serine/Arginine (SR)-rich linker and a C-terminal dimerization domain (CTD). Besides its involvement in oligomerization, the CTD of the N protein (N-CTD) is also able to bind to nucleic acids by itself, independent of the NTD. Here, we report the near-complete NMR backbone chemical shift assignments of the SARS-CoV-2 N-CTD to provide the basis for downstream applications, in particular site-resolved drug binding studies.

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