TY  - JOUR
A1  - Korn, Sophie
A1  - Lambertz, Roderick
A1  - Fürtig, Boris
A1  - Hengesbach, Martin
A1  - Löhr, Frank
A1  - Richter, Christian
A1  - Schwalbe, Harald
A1  - Weigand, Julia
A1  - Wöhnert, Jens
A1  - Schlundt, Andreas
T1  - 1H, 13C, and 15N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein
T2  - Biomolecular NMR assignments
N2  - The 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.
KW  - SARS-CoV-2
KW  - Structural protein
KW  - Nucleocapsid
KW  - Dimerization domain
KW  - Solution NMR-spectroscopy
KW  - Protein druggability
KW  - Covid19-NMR
Y1  - 2020
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/75713
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-757137
SN  - 1874-270X
N1  - The Frankfurt BMRZ (Center for Biomolecular Resonance) is supported by the Federal state of Hesse. This work was funded by the Deutsche Forschungsgemeinschaft through grant numbers SFB902/B18 (to Covid19-NMR), SCHL2062/2-1 (to A.S.), the Goethe University Corona funds and by the Johanna Quandt Young Academy at Goethe (grant number 2019/AS01 to A.S.).
Open Access funding enabled and organized by Projekt DEAL.
VL  - 15
IS  - 1
SP  - 129
EP  - 135
PB  - Springer
CY  - Dordrecht [u.a.]
ER  -