Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2
(2020) In International Journal of Molecular Sciences 21(19).- Abstract
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... (More)
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.
(Less)
- author
- organization
- publishing date
- 2020-10-06
- type
- Contribution to journal
- publication status
- published
- subject
- in
- International Journal of Molecular Sciences
- volume
- 21
- issue
- 19
- article number
- 7375
- pages
- 15 pages
- publisher
- MDPI AG
- external identifiers
-
- pmid:33036230
- scopus:85092227602
- ISSN
- 1422-0067
- DOI
- 10.3390/ijms21197375
- language
- English
- LU publication?
- yes
- id
- 9b21ff9c-37cc-4e50-8a2b-f241b4ce9d5a
- date added to LUP
- 2020-10-12 13:14:17
- date last changed
- 2024-09-19 06:35:42
@article{9b21ff9c-37cc-4e50-8a2b-f241b4ce9d5a, abstract = {{<p>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.</p>}}, author = {{Rogstam, Annika and Nyblom, Maria and Christensen, Signe and Sele, Celeste and Talibov, Vladimir O and Lindvall, Therese and Rasmussen, Anna Andersson and André, Ingemar and Fisher, Zoë and Knecht, Wolfgang and Kozielski, Frank}}, issn = {{1422-0067}}, language = {{eng}}, month = {{10}}, number = {{19}}, publisher = {{MDPI AG}}, series = {{International Journal of Molecular Sciences}}, title = {{Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2}}, url = {{http://dx.doi.org/10.3390/ijms21197375}}, doi = {{10.3390/ijms21197375}}, volume = {{21}}, year = {{2020}}, }