Next Article in Journal
Altered Gap Junction Network Topography in Mouse Models for Human Hereditary Deafness
Previous Article in Journal
Effect of Oral Losartan on Orthobiologics: Implications for Platelet-Rich Plasma and Bone Marrow Concentrate—A Rabbit Study
Article

Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2

1
Department of Biology & Lund Protein Production Platform, Lund University, Sölvegatan 35, 22362 Lund, Sweden
2
Department of Biochemistry and Structural Biology, Lund University, Naturvetarvägen 26, 22241 Lund, Sweden
3
BioMax, MAX IV Laboratory, Fotongatan 2, 22484 Lund, Sweden
4
Scientific Activities Division, Science Directorate, European Spallation Source ERIC, Box 176, SE-221 00 Lund, Sweden
5
School of Pharmacy, University College London, 29-39 Brunswick Square, London WC1N 1AX, UK
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(19), 7375; https://doi.org/10.3390/ijms21197375
Received: 14 September 2020 / Revised: 29 September 2020 / Accepted: 2 October 2020 / Published: 6 October 2020
(This article belongs to the Section Biochemistry)
Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2), causing Coronavirus Disease 19 (COVID-19), emerged at the end of 2019 and quickly spread to cause a global pandemic with severe socio-economic consequences. The early sequencing of its RNA genome revealed its high similarity to SARS, likely to have originated from bats. The SARS-CoV-2 non-structural protein 10 (nsp10) displays high sequence similarity with its SARS homologue, which binds to and stimulates the 3′-to-5′ exoribonuclease and the 2′-O-methlytransferase activities of nsps 14 and 16, respectively. Here, we report the biophysical characterization and 1.6 Å resolution structure of the unbound form of nsp10 from SARS-CoV-2 and compare it to the structures of its SARS homologue and the complex-bound form with nsp16 from SARS-CoV-2. The crystal structure and solution behaviour of nsp10 will not only form the basis for understanding the role of SARS-CoV-2 nsp10 as a central player of the viral RNA capping apparatus, but will also serve as a basis for the development of inhibitors of nsp10, interfering with crucial functions of the replication–transcription complex and virus replication. View Full-Text
Keywords: SARS CoV-2; COVID-19; non-structural proteins; nsp10; replication–transcription complex; RNA capping machinery SARS CoV-2; COVID-19; non-structural proteins; nsp10; replication–transcription complex; RNA capping machinery
Show Figures

Graphical abstract

MDPI and ACS Style

Rogstam, A.; Nyblom, M.; Christensen, S.; Sele, C.; Talibov, V.O.; Lindvall, T.; Rasmussen, A.A.; André, I.; Fisher, Z.; Knecht, W.; Kozielski, F. Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2. Int. J. Mol. Sci. 2020, 21, 7375. https://doi.org/10.3390/ijms21197375

AMA Style

Rogstam A, Nyblom M, Christensen S, Sele C, Talibov VO, Lindvall T, Rasmussen AA, André I, Fisher Z, Knecht W, Kozielski F. Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2. International Journal of Molecular Sciences. 2020; 21(19):7375. https://doi.org/10.3390/ijms21197375

Chicago/Turabian Style

Rogstam, Annika, Maria Nyblom, Signe Christensen, Celeste Sele, Vladimir O. Talibov, Therese Lindvall, Anna A. Rasmussen, Ingemar André, Zoë Fisher, Wolfgang Knecht, and Frank Kozielski. 2020. "Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2" International Journal of Molecular Sciences 21, no. 19: 7375. https://doi.org/10.3390/ijms21197375

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop