2bx3: Difference between revisions
New page: left|200px<br /><applet load="2bx3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bx3, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:2bx3.gif|left|200px]]<br /><applet load="2bx3" size=" | [[Image:2bx3.gif|left|200px]]<br /><applet load="2bx3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2bx3, resolution 2.00Å" /> | caption="2bx3, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE (P43212)'''<br /> | '''CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE (P43212)'''<br /> | ||
==Overview== | ==Overview== | ||
The SARS coronavirus main proteinase (M(pro)) is a key enzyme in the | The SARS coronavirus main proteinase (M(pro)) is a key enzyme in the processing of the viral polyproteins and thus an attractive target for the discovery of drugs directed against SARS. The enzyme has been shown by X-ray crystallography to undergo significant pH-dependent conformational changes. Here, we assess the conformational flexibility of the M(pro) by analysis of multiple crystal structures (including two new crystal forms) and by molecular dynamics (MD) calculations. The MD simulations take into account the different protonation states of two histidine residues in the substrate-binding site and explain the pH-activity profile of the enzyme. The low enzymatic activity of the M(pro) monomer and the need for dimerization are also discussed. | ||
==About this Structure== | ==About this Structure== | ||
2BX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http:// | 2BX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BX3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hilgenfeld, R.]] | [[Category: Hilgenfeld, R.]] | ||
[[Category: Mesters, J | [[Category: Mesters, J R.]] | ||
[[Category: Verschueren, K | [[Category: Verschueren, K H.G.]] | ||
[[Category: anti-parallel a-helices]] | [[Category: anti-parallel a-helices]] | ||
[[Category: anti-parallel b-barrel]] | [[Category: anti-parallel b-barrel]] | ||
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[[Category: viral protein]] | [[Category: viral protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:30 2008'' | ||
Revision as of 17:42, 21 February 2008
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CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE (P43212)
OverviewOverview
The SARS coronavirus main proteinase (M(pro)) is a key enzyme in the processing of the viral polyproteins and thus an attractive target for the discovery of drugs directed against SARS. The enzyme has been shown by X-ray crystallography to undergo significant pH-dependent conformational changes. Here, we assess the conformational flexibility of the M(pro) by analysis of multiple crystal structures (including two new crystal forms) and by molecular dynamics (MD) calculations. The MD simulations take into account the different protonation states of two histidine residues in the substrate-binding site and explain the pH-activity profile of the enzyme. The low enzymatic activity of the M(pro) monomer and the need for dimerization are also discussed.
About this StructureAbout this Structure
2BX3 is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.
ReferenceReference
pH-dependent conformational flexibility of the SARS-CoV main proteinase (M(pro)) dimer: molecular dynamics simulations and multiple X-ray structure analyses., Tan J, Verschueren KH, Anand K, Shen J, Yang M, Xu Y, Rao Z, Bigalke J, Heisen B, Mesters JR, Chen K, Shen X, Jiang H, Hilgenfeld R, J Mol Biol. 2005 Nov 18;354(1):25-40. Epub 2005 Sep 23. PMID:16242152
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