2c3s
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(New page: 200px<br /><applet load="2c3s" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c3s, resolution 1.9Å" /> '''STRUCTURE OF SARS COV...)
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Revision as of 06:52, 21 November 2007
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STRUCTURE OF SARS COV MAIN PROTEINASE AT 1.9 A (PH6.5)
Overview
The 34 kDa main proteinase (Mpro) from the severe acute respiratory, syndrome coronavirus (SARS-CoV) plays an important role in the virus life, cycle through the specific processing of viral polyproteins. As such, SARS-CoV Mpro is a key target for the identification of specific, inhibitors directed against the SARS virus. With a view to facilitating, the development of such compounds, crystals were obtained of the enzyme at, pH 6.5 in the orthorhombic space group P2(1)2(1)2 that diffract to a, resolution of 1.9 A. These crystals contain one monomer per asymmetric, unit and the biologically active dimer is generated via the, crystallographic twofold axis. The conformation of the catalytic site, indicates that the enzyme is active in the crystalline form and thus, suitable for structure-based inhibition studies.
About this Structure
2C3S is a Single protein structure of sequence from Human sars coronavirus. This structure superseeds the now removed PDB entry 2BW6. Full crystallographic information is available from OCA.
Reference
Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer., Xu T, Ooi A, Lee HC, Wilmouth R, Liu DX, Lescar J, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Nov 1;61(Pt, 11):964-6. Epub 2005 Oct 20. PMID:16511208
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