*nlm.life
			PubMed Journals: Science

  Source:		PMID: 12746549


    		Science. 2003 Jun 13;300(5626):1763-7. Epub
     		2003 May 13.

			Coronavirus main proteinase (3CLpro) structure:
			basis for design of anti-SARS drugs.

			Anand K(1), Ziebuhr J, Wadhwani P, Mesters
			JR, Hilgenfeld R.

			Author Information
			(1) Institute of Biochemistry, University
			of Lübeck, D-23538 Lübeck, Germany.

			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.

			DOI: 10.1126/science.1085658 PMID: 12746549
			[Indexed for MEDLINE]

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