TY  - JOUR
A1  - Kubatova, Nina
A1  - Qureshi, Nusrat
A1  - Altınçekiç, Nadide
A1  - Abele, Rupert
A1  - Bains, Jasleen Kaur
A1  - Ceylan, Betül
A1  - Ferner, Jan
A1  - Fuks, Christin
A1  - Hargittay, Bruno
A1  - Hutchison, Marie
A1  - de Jesus, Vanessa
A1  - Kutz, Felicitas
A1  - Wirtz Martin, Maria Alexandra
A1  - Meiser, Nathalie
A1  - Linhard, Verena
A1  - Pyper, Dennis Joshua
A1  - Trucks, Sven
A1  - Fürtig, Boris
A1  - Hengesbach, Martin
A1  - Löhr, Frank
A1  - Richter, Christian
A1  - Saxena, Krishna
A1  - Schlundt, Andreas
A1  - Schwalbe, Harald
A1  - Sreeramulu, Sridhar
A1  - Wacker, Anna
A1  - Weigand, Julia
A1  - Wirmer-Bartoschek, Julia
A1  - Wöhnert, Jens
T1  - 1H, 13C, and 15N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10
T2  - Biomolecular NMR assignments
N2  - The international Covid19-NMR consortium aims at the comprehensive spectroscopic characterization of SARS-CoV-2 RNA elements and proteins and will provide NMR chemical shift assignments of the molecular components of this virus. The SARS-CoV-2 genome encodes approximately 30 different proteins. Four of these proteins are involved in forming the viral envelope or in the packaging of the RNA genome and are therefore called structural proteins. The other proteins fulfill a variety of functions during the viral life cycle and comprise the so-called non-structural proteins (nsps). Here, we report the near-complete NMR resonance assignment for the backbone chemical shifts of the non-structural protein 10 (nsp10). Nsp10 is part of the viral replication-transcription complex (RTC). It aids in synthesizing and modifying the genomic and subgenomic RNAs. Via its interaction with nsp14, it ensures transcriptional fidelity of the RNA-dependent RNA polymerase, and through its stimulation of the methyltransferase activity of nsp16, it aids in synthesizing the RNA cap structures which protect the viral RNAs from being recognized by the innate immune system. Both of these functions can be potentially targeted by drugs. Our data will aid in performing additional NMR-based characterizations, and provide a basis for the identification of possible small molecule ligands interfering with nsp10 exerting its essential role in viral replication.
KW  - SARS-CoV-2
KW  - Non-structural protein
KW  - Solution NMR-spectroscopy
KW  - Covid19-NMR
Y1  - 2020
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/79513
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-795137
SN  - 1874-270X
N1  - Work at BMRZ is supported by the state of Hesse. Work in Covid19-NMR was supported by the Goethe Corona Funds, and by the DFG within the SFB902.
Open Access funding enabled and organized by Projekt DEAL.
VL  - 15
IS  - 1
SP  - 65
EP  - 71
PB  - Springer Netherlands
CY  - Dordrecht [u.a.]
ER  -