"552987" . "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-triphosphate (ATP) ?-phosphate to serine or threonine hydroxyl in the protein substrate. The CDK2 activity is regulated by complex mechanism including binding to positive regulatory subunit (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 inhibitors [2,3], 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 dynami"@en . . . "MD studie CDK2"@cs . "MD studie CDK2"@cs . "Z(MSM 143100005)" . "3"^^ . "4"^^ . "Otyepka, Michal" . . . . . "260-261" . "2"^^ . . . "MD studie CDK2"@cs . "Ko\u010Da, Jaroslav" . "Olomouc" . . "Olomouc" . "A MOLECULAR DYNAMICS STUDY OF THE CYCLIN-DEPENDENT KINASE-2 (CDK2) WITH SUBSTRATE PEPTIDE (HHASPRK) INHIBITION BY PHOSPHORYLATION" . "2004-01-01+01:00"^^ . "Acta Univ. Palacki. Olomouc., Fac. Rer. Nat., Chemica 43S" . "[9AD2169C53D8]" . . "A MOLECULAR DYNAMICS STUDY OF THE CYCLIN-DEPENDENT KINASE-2 (CDK2) WITH SUBSTRATE PEPTIDE (HHASPRK) INHIBITION BY PHOSPHORYLATION"@en . "14310" . . "cell cycle; CDK regulation; phosphorylated tyrosine; threonine"@en . "A MOLECULAR DYNAMICS STUDY OF THE CYCLIN-DEPENDENT KINASE-2 (CDK2) WITH SUBSTRATE PEPTIDE (HHASPRK) INHIBITION BY PHOSPHORYLATION" . . "RIV/00216224:14310/04:00010531!RIV08-MSM-14310___" . . . "B\u00E1rtov\u00E1, Iveta" . "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-triphosphate (ATP) ?-phosphate to serine or threonine hydroxyl in the protein substrate. The CDK2 activity is regulated by complex mechanism including binding to positive regulatory subunit (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 inhibitors [2,3], 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 dynami" . . "80-244-0353-6" . "K\u0159\u00ED\u017E, Zden\u011Bk" . . "A MOLECULAR DYNAMICS STUDY OF THE CYCLIN-DEPENDENT KINASE-2 (CDK2) WITH SUBSTRATE PEPTIDE (HHASPRK) INHIBITION BY PHOSPHORYLATION"@en . . . "Univerzita Palack\u00E9ho v Olomouci" . "RIV/00216224:14310/04:00010531" . .