1cqq: Difference between revisions

Revision as of 21:09, 30 June 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:1cqq.png

Template:STRUCTURE 1cqq

TYPE 2 RHINOVIRUS 3C PROTEASE WITH AG7088 INHIBITORTYPE 2 RHINOVIRUS 3C PROTEASE WITH AG7088 INHIBITOR

Template:ABSTRACT PUBMED 10500114

About this StructureAbout this Structure

1CQQ is a Single protein structure of sequence from Human rhinovirus 2. Full crystallographic information is available from OCA.

ReferenceReference

Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes., Matthews DA, Dragovich PS, Webber SE, Fuhrman SA, Patick AK, Zalman LS, Hendrickson TF, Love RA, Prins TJ, Marakovits JT, Zhou R, Tikhe J, Ford CE, Meador JW, Ferre RA, Brown EL, Binford SL, Brothers MA, DeLisle DM, Worland ST, Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11000-7. PMID:10500114

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OCA

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-'''TYPE 2 RHINOVIRUS 3C PROTEASE WITH AG7088 INHIBITOR'''
+===TYPE 2 RHINOVIRUS 3C PROTEASE WITH AG7088 INHIBITOR===
-==Overview==
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-Human rhinoviruses, the most important etiologic agents of the common cold, are messenger-active single-stranded monocistronic RNA viruses that have evolved a highly complex cascade of proteolytic processing events to control viral gene expression and replication. Most maturation cleavages within the precursor polyprotein are mediated by rhinovirus 3C protease (or its immediate precursor, 3CD), a cysteine protease with a trypsin-like polypeptide fold. High-resolution crystal structures of the enzyme from three viral serotypes have been used for the design and elaboration of 3C protease inhibitors representing different structural and chemical classes. Inhibitors having alpha,beta-unsaturated carbonyl groups combined with peptidyl-binding elements specific for 3C protease undergo a Michael reaction mediated by nucleophilic addition of the enzyme's catalytic Cys-147, resulting in covalent-bond formation and irreversible inactivation of the viral protease. Direct inhibition of 3C proteolytic activity in virally infected cells treated with these compounds can be inferred from dose-dependent accumulations of viral precursor polyproteins as determined by SDS/PAGE analysis of radiolabeled proteins. Cocrystal-structure-assisted optimization of 3C-protease-directed Michael acceptors has yielded molecules having extremely rapid in vitro inactivation of the viral protease, potent antiviral activity against multiple rhinovirus serotypes and low cellular toxicity. Recently, one compound in this series, AG7088, has entered clinical trials.
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+{{ABSTRACT_PUBMED_10500114}}
 ==About this Structure==
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 [[Category: Matthews, D.]]
 [[Category: Viral protein]]
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