%0 Journal Article %1 Anand1763 %A Anand, Kanchan %A Ziebuhr, John %A Wadhwani, Parvesh %A Mesters, Jeroen R. %A Hilgenfeld, Rolf %D 2003 %I American Association for the Advancement of Science %J Science %K 3CLPro SARS_1 %N 5626 %P 1763--1767 %R 10.1126/science.1085658 %T Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of Anti-SARS Drugs %U https://science.sciencemag.org/content/300/5626/1763 %V 300 %X A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (Mpro, also called 3CLpro), which controls the activities of the coronavirus replication complex, is an attractive target for therapy. We determined crystal structures for human coronavirus (strain 229E) Mpro and for an inhibitor complex of porcine coronavirus transmissible gastroenteritis virus (TGEV) Mpro, and we constructed a homology model for SARS coronavirus (SARS-CoV) Mpro. The structures reveal a remarkable degree of conservation of the substrate-binding sites, which is further supported by recombinant SARS-CoV Mpro-mediated cleavage of a TGEV Mpro substrate. Molecular modeling suggests that available rhinovirus 3Cpro inhibitors may be modified to make them useful for treating SARS.

@article{Anand1763, abstract = {A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (Mpro, also called 3CLpro), which controls the activities of the coronavirus replication complex, is an attractive target for therapy. We determined crystal structures for human coronavirus (strain 229E) Mpro and for an inhibitor complex of porcine coronavirus [transmissible gastroenteritis virus (TGEV)] Mpro, and we constructed a homology model for SARS coronavirus (SARS-CoV) Mpro. The structures reveal a remarkable degree of conservation of the substrate-binding sites, which is further supported by recombinant SARS-CoV Mpro-mediated cleavage of a TGEV Mpro substrate. Molecular modeling suggests that available rhinovirus 3Cpro inhibitors may be modified to make them useful for treating SARS.}, added-at = {2021-02-21T13:34:40.000+0100}, author = {Anand, Kanchan and Ziebuhr, John and Wadhwani, Parvesh and Mesters, Jeroen R. and Hilgenfeld, Rolf}, biburl = {https://www.bibsonomy.org/bibtex/2cc4e6756a3cabbec8466284c570cac6d/fordham1}, description = {Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of Anti-SARS Drugs | Science}, doi = {10.1126/science.1085658}, eprint = {https://science.sciencemag.org/content/300/5626/1763.full.pdf}, interhash = {026282b424f486b25d09ba618361a15b}, intrahash = {cc4e6756a3cabbec8466284c570cac6d}, issn = {0036-8075}, journal = {Science}, keywords = {3CLPro SARS_1}, number = 5626, pages = {1763--1767}, publisher = {American Association for the Advancement of Science}, timestamp = {2021-02-21T13:34:40.000+0100}, title = {Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of Anti-SARS Drugs}, url = {https://science.sciencemag.org/content/300/5626/1763}, volume = 300, year = 2003 }