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 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.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Rogstam A,Nyblom M,Christensen S,Sele C,Talibov VO,Lindvall T,Rasmussen AA,André I,Fisher Z,Knecht W,Kozielski Fdoi
10.3390/ijms21197375subject
Has Abstractpub_date
2020-10-06 00:00:00issue
19issn
1422-0067pii
ijms21197375journal_volume
21pub_type
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