2gz7: Difference between revisions

Revision as of 01:56, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2gz7.png

Template:STRUCTURE 2gz7

Structure-Based Drug Design and Structural Biology Study of Novel Nonpeptide Inhibitors of SARS-CoV Main ProteaseStructure-Based Drug Design and Structural Biology Study of Novel Nonpeptide Inhibitors of SARS-CoV Main Protease

Template:ABSTRACT PUBMED 16913704

About this StructureAbout this Structure

2GZ7 is a Single protein structure of sequence from Sars coronavirus. Full crystallographic information is available from OCA.

ReferenceReference

Structure-based drug design and structural biology study of novel nonpeptide inhibitors of severe acute respiratory syndrome coronavirus main protease., Lu IL, Mahindroo N, Liang PH, Peng YH, Kuo CJ, Tsai KC, Hsieh HP, Chao YS, Wu SY, J Med Chem. 2006 Aug 24;49(17):5154-61. PMID:16913704

Page seeded by OCA on Mon Jul 28 01:56:40 2008

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OCA

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-'''Structure-Based Drug Design and Structural Biology Study of Novel Nonpeptide Inhibitors of SARS-CoV Main Protease'''
+===Structure-Based Drug Design and Structural Biology Study of Novel Nonpeptide Inhibitors of SARS-CoV Main Protease===
-==Overview==
+<!--
-Severe acute respiratory syndrome coronavirus (SARS-CoV) main protease (M(pro)), a protein required for the maturation of SARS-CoV, is vital for its life cycle, making it an attractive target for structure-based drug design of anti-SARS drugs. The structure-based virtual screening of a chemical database containing 58,855 compounds followed by the testing of potential compounds for SARS-CoV M(pro) inhibition leads to two hit compounds. The core structures of these two hits, defined by the docking study, are used for further analogue search. Twenty-one analogues derived from these two hits exhibited IC50 values below 50 microM, with the most potent one showing 0.3 microM. Furthermore, the complex structures of two potent inhibitors with SARS-CoV M(pro) were solved by X-ray crystallography. They bind to the protein in a distinct manner compared to all published SARS-CoV M(pro) complex structures. They inhibit SARS-CoV M(pro) activity via intensive H-bond network and hydrophobic interactions, without the formation of a covalent bond. Interestingly, the most potent inhibitor induces protein conformational changes, and the inhibition mechanisms, particularly the disruption of catalytic dyad (His41 and Cys145), are elaborated.
+The line below this paragraph, {{ABSTRACT_PUBMED_16913704}}, adds the Publication Abstract to the page
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 [[Category: Wu, S Y.]]
 [[Category: Sars cov main protease]]
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