"14310" . "2003-01-01+01:00"^^ . . "COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION"@cs . "RIV/00216224:14310/03:00009258!RIV08-MSM-14310___" . . "Workshop on Modeling Interactions in Biomolecules" . . "Praha" . . "601948" . . "P(LN00A016)" . "COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION"@en . . . . . "COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION"@cs . . "Book of Abstracts" . . . "Otyepka, Michal" . "Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. Cell-cycle dependent oscillations in CDK activity are induced by complex mechanisms that include binding to positive regulatory subunits and phosphorylation at positive and negative regulatory sites. Binding to Cyclin A or Cyclin E is required for CDK2 activation. CDK2 obtains full activity by phosphorylation of the T160 residue in the activation segment (T-loop) and it is inhibited by phosphorylation on inhibitory sites at Y15 and/or T14 in the Glycine rich loop (G-loop). CDK2 is inhibited also by interactions with various native protein inhibitors. The primary function of CDK is to catalyze the phosphoryl transfer of the ATP g-phosphate to serine or threonine hydroxyl in the protein target substrate. The adenosine triphosphate is native substrate of CDK2. Human CDK2 contains the classical bi-lobal kinase fold. The ATP binding site is located in the deep cleft between two lobes. The N-terminal domain is composed mainly"@cs . "[025FA618970D]" . . "Ko\u010Da, Jaroslav" . "4"^^ . "COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION" . "RIV/00216224:14310/03:00009258" . . "COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION" . "Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. Cell-cycle dependent oscillations in CDK activity are induced by complex mechanisms that include binding to positive regulatory subunits and phosphorylation at positive and negative regulatory sites. Binding to Cyclin A or Cyclin E is required for CDK2 activation. CDK2 obtains full activity by phosphorylation of the T160 residue in the activation segment (T-loop) and it is inhibited by phosphorylation on inhibitory sites at Y15 and/or T14 in the Glycine rich loop (G-loop). CDK2 is inhibited also by interactions with various native protein inhibitors. The primary function of CDK is to catalyze the phosphoryl transfer of the ATP g-phosphate to serine or threonine hydroxyl in the protein target substrate. The adenosine triphosphate is native substrate of CDK2. Human CDK2 contains the classical bi-lobal kinase fold. The ATP binding site is located in the deep cleft between two lobes. The N-terminal domain is composed mainly" . . . "Nov\u00E9 Hrady" . "3"^^ . "K\u0159\u00ED\u017E, Zden\u011Bk" . "1"^^ . . "8" . "COMPUTER SIMULATIONS OF CYCLIN-DEPENDENT KINASE-2 NOTES ABOUT INHIBITION"@en . "Cyclin-dependent kinases (CDKs) are enzymes controlling the eukaryotic cell cycle. Cell-cycle dependent oscillations in CDK activity are induced by complex mechanisms that include binding to positive regulatory subunits and phosphorylation at positive and negative regulatory sites. Binding to Cyclin A or Cyclin E is required for CDK2 activation. CDK2 obtains full activity by phosphorylation of the T160 residue in the activation segment (T-loop) and it is inhibited by phosphorylation on inhibitory sites at Y15 and/or T14 in the Glycine rich loop (G-loop). CDK2 is inhibited also by interactions with various native protein inhibitors. The primary function of CDK is to catalyze the phosphoryl transfer of the ATP g-phosphate to serine or threonine hydroxyl in the protein target substrate. The adenosine triphosphate is native substrate of CDK2. Human CDK2 contains the classical bi-lobal kinase fold. The ATP binding site is located in the deep cleft between two lobes. The N-terminal domain is composed mainly"@en . "B\u00E1rtov\u00E1, Iveta" . . "molekular dynamics; CDK regulation; cell cycle"@en .