"Je diskutov\u00E1na molekulov\u00E1 dynamika CDK2 se substr\u00E1tov\u00FDm peptidem HHASPRK a inhibice fosforylac\u00ED."@cs . . "K\u0159\u00ED\u017E, Zden\u011Bk" . . "RIV/61989592:15310/04:00002046" . "[00710A2DB1F7]" . "Molekulov\u00E1 dynamika CDK2 se substr\u00E1tov\u00FDm peptidem HHASPRK, inhibice fosforylac\u00ED"@cs . . . "0232-0061" . "Otyepka, Michal" . "Molekulov\u00E1 dynamika CDK2 se substr\u00E1tov\u00FDm peptidem HHASPRK, inhibice fosforylac\u00ED"@cs . "552986" . . "A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation" . "cyclic dependent kinase;CDK2;inhibition;phosphorylation"@en . "The cyclin-dependent kinase-2, CDK2, controls the eukaryotic cell cycle at the G1 -S boundary. CDK2 catalyzes the phosphoryl transfer of the adenosine-5\u00B4-triphosphate (ATP) ?-phosphate to serine or threonine hydroxyl in the protein substrate. The CDK2 activity is regulated by complex mechanism including binding to positive regulatorysubunit (Cyclin A or Cyclin E) and phosphorylation at positive regulatory site in the activation segment (T-loop)1. The CDK2 activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various artificial and natural protein inhibitors2,3, etc. The CDK2 can be also negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 residue in the inhibition segment (G-loop)4. Mechanism of the CDK2 inhibition by phosphorylation is known from the kinetics experiments but the structural aspects of inhibition remains unclear. The first attempt to explain the mechanism of inhibition by phosphorylation came from molecular dynamics simul" . "43" . . "A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation"@en . "CZ - \u010Cesk\u00E1 republika" . "260" . "The cyclin-dependent kinase-2, CDK2, controls the eukaryotic cell cycle at the G1 -S boundary. CDK2 catalyzes the phosphoryl transfer of the adenosine-5\u00B4-triphosphate (ATP) ?-phosphate to serine or threonine hydroxyl in the protein substrate. The CDK2 activity is regulated by complex mechanism including binding to positive regulatorysubunit (Cyclin A or Cyclin E) and phosphorylation at positive regulatory site in the activation segment (T-loop)1. The CDK2 activity is inhibited in several ways, for example, by (de)phosphorylation, interaction with various artificial and natural protein inhibitors2,3, etc. The CDK2 can be also negatively regulated by phosphorylation at Y15 and, to a lesser extent, at T14 residue in the inhibition segment (G-loop)4. Mechanism of the CDK2 inhibition by phosphorylation is known from the kinetics experiments but the structural aspects of inhibition remains unclear. The first attempt to explain the mechanism of inhibition by phosphorylation came from molecular dynamics simul"@en . . . "Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica" . . "1"^^ . "4"^^ . "B\u00E1rtov\u00E1, Iveta" . . "Suppl." . "Z(MSM 153100007)" . "A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation" . . . . "275"^^ . "A molecular dynamics study of the cyclin-dependent kinase-2 (CDK2) with substrate peptide (HHASPRK) inhibition by phosphorylation"@en . . . "15310" . "Ko\u010Da, Jaroslav" . . "RIV/61989592:15310/04:00002046!RIV/2005/MSM/153105/N" .