Filgueira de Azevedo Jr., Walter [UNESP]Canduri, Fernanda [UNESP]Freitas da Silveira, Nelson José [UNESP]2014-05-272014-05-272002-07-08Biochemical and Biophysical Research Communications, v. 293, n. 1, p. 566-571, 2002.0006-291Xhttp://hdl.handle.net/11449/66932Flavopiridol 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.566-571engBioinformaticsCDKDrug designFlavopiridolStructure2,6 diamino 4 cyclohexylmethoxy 5 nitrosopyrimidine6 n (3,3 dimethylallyl)adenine6 o cyclohexylmethylguanineadenine derivativeadenosine triphosphatecyclin dependent kinasecyclin dependent kinase 2cyclin dependent kinase 9cyclin T1dechloroflavopiridolenzyme inhibitorflavone derivativeflavopiridolhymenialdisineindirubinolomoucinepkfo 49 38purvalanol Broscovitinestaurosporineu 55unclassified drugcorrelation analysisdrug potencydrug protein bindingdrug structureenzyme inhibitionIC 50molecular modelpriority journalstructure activity relationstructure analysisAmino Acid SequenceCyclin-Dependent Kinase 9Cyclin-Dependent KinasesEnzyme InhibitorsFlavonoidsModels, MolecularMolecular Sequence DataPiperidinesProtein ConformationSequence AlignmentSequence Homology, Amino AcidArtigo10.1016/S0006-291X(02)00266-8WOS:000175514700086Acesso restrito2-s2.0-0036295220