2bx4

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{{STRUCTURE_2bx4| PDB=2bx4 | SCENE= }}
{{STRUCTURE_2bx4| PDB=2bx4 | SCENE= }}
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'''CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE (P21212)'''
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===CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE (P21212)===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16242152 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16242152}}
==About this Structure==
==About this Structure==
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[[Category: Sar]]
[[Category: Sar]]
[[Category: Viral protein]]
[[Category: Viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:34:49 2008''

Revision as of 15:34, 27 July 2008

Image:2bx4.png

Template:STRUCTURE 2bx4

CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE (P21212)

Template:ABSTRACT PUBMED 16242152

About this Structure

2BX4 is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.

Reference

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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