1P9S: Coronavirus Main Proteinase (3clpro) Structure: Basis For Design Of Anti-sars Drugs

Citation:
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.
PDB ID: 1P9SDownload
MMDB ID: 23158
PDB Deposition Date: 2003/5/12
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.54  Å
Source Organism:
Similar Structures:
Biological Unit for 1P9S: monomeric; determined by author
Molecular Components in 1P9S
Label Count Molecule
Protein (1 molecule)
1
Replicase Polyprotein 1AB
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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