2bx3: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bx3 OCA], [http://www.ebi.ac.uk/pdbsum/2bx3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bx3 RCSB]</span> | |||
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:13:09 2008'' | ||
Revision as of 02:13, 31 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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