Structural basis for inhibition of cyclin-dependent kinase 9 by flavopiridol

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dc.contributor.authorFilgueira de Azevedo Jr., Walter [UNESP]
dc.contributor.authorCanduri, Fernanda [UNESP]
dc.contributor.authorFreitas da Silveira, Nelson José [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-27T11:20:29Z
dc.date.available2014-05-27T11:20:29Z
dc.date.issued2002-07-08
dc.description.abstractFlavopiridol has been shown to potently inhibit CDK1 and 2 (cyclin-dependent kinases 1 and 2) and most recently it has been found that it also inhibits CDK9. The complex CDK9-cyclin T1 controls the elongation phase of transcription by RNA polymerase II. The present work describes a molecular model for the binary complex CDK9-flavopiridol. This structural model indicates that the inhibitor strongly binds to the ATP-binding pocket of CDK9 and the structural comparison of the complex CDK2-flavopiridol correlates the structural differences with differences in inhibition of these CDKs by flavopiridol. This structure opens the possibility of testing new inhibitor families, in addition to new substituents for the already known leading structures such as flavones and adenine derivatives. © 2002 Elsevier Science (USA). All rights reserved.en
dc.description.affiliationDepartamento de Física IBILCE UNESP, Sao Jose do Rio Preto, SP 15054-000
dc.description.affiliationUnespDepartamento de Física IBILCE UNESP, Sao Jose do Rio Preto, SP 15054-000
dc.format.extent566-571
dc.identifierhttp://dx.doi.org/10.1016/S0006-291X(02)00266-8
dc.identifier.citationBiochemical and Biophysical Research Communications, v. 293, n. 1, p. 566-571, 2002.
dc.identifier.doi10.1016/S0006-291X(02)00266-8
dc.identifier.issn0006-291X
dc.identifier.scopus2-s2.0-0036295220
dc.identifier.urihttp://hdl.handle.net/11449/66932
dc.identifier.wosWOS:000175514700086
dc.language.isoeng
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.relation.ispartofjcr2.559
dc.rights.accessRightsAcesso restrito
dc.sourceScopus
dc.subjectBioinformatics
dc.subjectCDK
dc.subjectDrug design
dc.subjectFlavopiridol
dc.subjectStructure
dc.subject2,6 diamino 4 cyclohexylmethoxy 5 nitrosopyrimidine
dc.subject6 n (3,3 dimethylallyl)adenine
dc.subject6 o cyclohexylmethylguanine
dc.subjectadenine derivative
dc.subjectadenosine triphosphate
dc.subjectcyclin dependent kinase
dc.subjectcyclin dependent kinase 2
dc.subjectcyclin dependent kinase 9
dc.subjectcyclin T1
dc.subjectdechloroflavopiridol
dc.subjectenzyme inhibitor
dc.subjectflavone derivative
dc.subjectflavopiridol
dc.subjecthymenialdisine
dc.subjectindirubin
dc.subjectolomoucine
dc.subjectpkfo 49 38
dc.subjectpurvalanol B
dc.subjectroscovitine
dc.subjectstaurosporine
dc.subjectu 55
dc.subjectunclassified drug
dc.subjectcorrelation analysis
dc.subjectdrug potency
dc.subjectdrug protein binding
dc.subjectdrug structure
dc.subjectenzyme inhibition
dc.subjectIC 50
dc.subjectmolecular model
dc.subjectpriority journal
dc.subjectstructure activity relation
dc.subjectstructure analysis
dc.subjectAmino Acid Sequence
dc.subjectCyclin-Dependent Kinase 9
dc.subjectCyclin-Dependent Kinases
dc.subjectEnzyme Inhibitors
dc.subjectFlavonoids
dc.subjectModels, Molecular
dc.subjectMolecular Sequence Data
dc.subjectPiperidines
dc.subjectProtein Conformation
dc.subjectSequence Alignment
dc.subjectSequence Homology, Amino Acid
dc.titleStructural basis for inhibition of cyclin-dependent kinase 9 by flavopiridolen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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