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1p9u

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(New page: 200px<br /><applet load="1p9u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9u, resolution 2.37&Aring;" /> '''Coronavirus Main Pro...)
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Revision as of 21:30, 20 November 2007

Image:1p9u.gif

1p9u, resolution 2.37Å

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

Overview

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.

About this Structure

1P9U is a Single protein structure of sequence from Transmissible gastroenteritis virus with SO4, CH2 and MRD as ligands. Full crystallographic information is available from OCA.

Reference

Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs., Anand K, Ziebuhr J, Wadhwani P, Mesters JR, Hilgenfeld R, Science. 2003 Jun 13;300(5626):1763-7. Epub 2003 May 13. PMID:12746549

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