TY  - JOUR
A1  - Korn, Sophie
A1  - Dhamotharan, Karthikeyan
A1  - Fürtig, Boris
A1  - Hengesbach, Martin
A1  - Löhr, Frank
A1  - Qureshi, Nusrat
A1  - Richter, Christian
A1  - Saxena, Krishna
A1  - Schwalbe, Harald
A1  - Tants, Jan-Niklas
A1  - Weigand, Julia
A1  - Wöhnert, Jens
A1  - Schlundt, Andreas
T1  - 1H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e
T2  - Biomolecular NMR assignments
N2  - 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.
KW  - SARS-CoV-2
KW  - Non-structural protein
KW  - Nucleic acid-binding domain
KW  - Solution NMR-spectroscopy
KW  - Protein drugability
KW  - Covid19-NMR
Y1  - 2020
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/69451
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-694517
SN  - 1874-270X
N1  - Open Access funding provided by Projekt DEAL. The Frankfurt BMRZ (Center for Biomolecular Resonance) is supported by the Federal state of Hesse.
N1  - This work was funded by the Deutsche Forschungsgemeinschaft through grant numbers SFB902/B18 (to covid19-nmr), SCHL2062/2 − 1 (to A.S.), and by the Johanna Quandt Young Academy at Goethe (Grant Number 2019/AS01 to A.S.).
N1  - The chemical shift values for the 1H, 13C and 15N resonances of SARS-CoV-2 Nsp3e have been deposited at the BioMagResBank (https://www.bmrb.wisc.edu) under accession number 50334. Spectral raw data (upon request) and assignments are also accessible through https://covid19-nmr.de.
VL  - 14
IS  - 2
SP  - 329
EP  - 333
PB  - Springer Netherlands
CY  - Dordrecht [u.a.]
ER  -