1P9S

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

Summary for 1P9S

• Entry DOI: 10.2210/pdb1p9s/pdb
• Related: 1LVO 1P9T 1P9U
• Descriptor: Replicase polyprotein 1ab, 1,4-DIETHYLENE DIOXIDE (3 entities in total)
• Functional Keywords: sars-cov, hcov, coronavirus, tgev, hydrolase
• Biological source: Human coronavirus
• Total number of polymer chains: 2
• Total formula weight: 66798.68

Authors

Anand, K.,Ziebuhr, J.,Wadhwani, P.,Mesters, J.R.,Hilgenfeld, R. (deposition date: 2003-05-12, release date: 2003-05-20, Last modification date: 2024-10-30)

Primary citation

Anand, K.,Ziebuhr, J.,Wadhwani, P.,Mesters, J.R.,Hilgenfeld, R.
Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of anti-SARS Drugs
Science, 300:1763-1767, 2003

PubMed 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.

PubMed: 12746549
DOI: 10.1126/science.1085658

Experimental method

X-RAY DIFFRACTION (2.54 Å)