The crystal structure of nsp10-nsp16 heterodimer from SARS CoV-2in complex with S-adenosylmethionine
Rosas Lemus, M.; Minasov, G.; Shuvalova, L.; Inniss, N. L.; Kiryukhina, O.; Wiersum, G.; Kim, Y.; Jedrzejczak, R.; Enders, M.; Jaroszewski, L.; Godzik, A.; Joachimiak, A.; Satchell, K. J.
Show abstract
SARS-CoV-2 is a member of the coronaviridae family and is the etiological agent of the respiratory Coronavirus Disease 2019. The virus has spread rapidly around the world resulting in over two million cases and nearly 150,000 deaths as of April 17, 2020. Since no treatments or vaccines are available to treat COVID-19 and SARS-CoV-2, respiratory complications derived from the infections have overwhelmed healthcare systems around the world. This virus is related to SARS-CoV-1, the virus that caused the 2002-2004 outbreak of Severe Acute Respiratory Syndrome. In January 2020, the Center for Structural Genomics of Infectious Diseases implemented a structural genomics pipeline to solve the structures of proteins essential for coronavirus replication-transcription. Here we show the first structure of the SARS-CoV-2 nsp10-nsp16 2-O-methyltransferase complex with S-adenosylmethionine at a resolution of 1.80 [A]. This heterodimer complex is essential for capping viral mRNA transcripts for efficient translation and to evade immune surveillance.
Matching journals
The top 6 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- A fold switch regulates conformation of an alphavirus virus RNA-dependent RNA polymerase 97%
- Structural and functional characterization of the Severe fever with thrombocytopenia syndrome virus L protein 96%
- Allosteric regulation and crystallographic fragment screening of SARS-CoV-2 NSP15 endoribonuclease 96%
Similar papers in this journal
- Structure of VanS from Vancomycin-Resistant Enterococci: A Sensor Kinase with Weak ATP Binding 96%
- Molecular architecture and domain arrangement of the placental malaria protein VAR2CSA suggests a model for receptor binding 95%
- Determinants of receptor tyrosine phosphatase homophilic adhesion: structural comparison of PTPRK and PTPRM extracellular domains 95%
Similar papers in this journal
- Structure and dynamics of SARS-CoV-2 proofreading exoribonuclease ExoN 96%
- Structure-function analysis of the nsp14 N7-guanine methyltransferase reveals an essential role in Betacoronavirus replication 95%
- Structural convergence for tubulin binding of CPAP and vinca domain microtubule inhibitors 95%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.