Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of Anti-SARS Drugs

By K. Anand, J. Ziebuhr, P. Wadhwani, J. Mesters, Rolf Hilgenfeld. Science, 2003

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The SARS-CoV-2 main protease as drug target (2020, positive): “Amongst the coronaviral targets that have been studied in the past, the main protease (Mpro, 3CLpro, nsp5) received major attention,25,56 particularly following the first SARS-CoV outbreak in the early 2000s.(23,57) Alternative coronaviral targets include the spike protein (S), RNA-de-”
New design strategies for antidepressant drugs (2013, background): “Micromolar affinities for VS hit compounds are not uncommon when homology models are employed [112-118], especially given the low sequence identity (< 30%) between LeuT and hSERT.”
Coronaviruses post-SARS: Update on replication and pathogenesis (2009, background): “The structure of many of these proteins has been solved by X-ray crystallography or nuclear magnetic resonance, facilitating structure-function studies [30] [31] [32] [33] [34] [35] [36] [37] [38] [39] [40] .”
Nidovirales: Evolving the largest RNA virus genome (2006, background): “The crystal structures of oronavirus and arterivirus 3CLpros revealed that both groups f enzymes have a three-domain structure, with domains I and I forming a (chymotrypsin-like) two-ß-barrel fold consisting f 12 or 13 ß-strands (Anand et al., 2002, 2003; Barrette-Ng t al., 2002; Yang et al., 2003).”
Mechanisms and enzymes involved in SARS coronavirus genome expression. (2003, background): “the only coronavirus protein for which structure information is available ( Anand et al., 2002, 2003 ).”