. "4"^^ . . "11" . "0021-9258" . "DIFFERENT MECHANISMS OF CDK5 AND CDK2 ACTIVATION AS REVEALED BY CDK5/P25 AND CDK2/CYCLIN A DYNAMICS"@en . "DIFFERENT MECHANISMS OF CDK5 AND CDK2 ACTIVATION AS REVEALED BY CDK5/P25 AND CDK2/CYCLIN A DYNAMICS" . . . "A detailed analysis is presented of the dynamics of human CDK5 in complexes with the protein activator p25 and the purine-like inhibitor roscovitine. These, and other findings related to the activation of CDK5 are critically reviewed from a molecular perspective. In addition, the results obtained on the behavior of CDK5 are compared to data on CDK2 to assess the differences and similarities between the two kinases in terms of (i) roscovitine binding, (ii) regulatory subunit association, (iii) conformational changes in the T-loop following CDK/regulatory subunit complex formation and (iv) specificity in CDK/regulatory subunit recognition. An energy decomposition analysis, used for these purposes, revealed why the binding of p25 alone is sufficient to stabilize the extended active T-loop conformation of CDK5, whereas the equivalent conformational change in CDK2 requires both the binding of Cyclin A and phosphorylation of the Thr160 residue." . . "DIFFERENT MECHANISMS OF CDK5 AND CDK2 ACTIVATION AS REVEALED BY CDK5/P25 AND CDK2/CYCLIN A DYNAMICS"@en . . "DIFFERENT MECHANISMS OF CDK5 AND CDK2 ACTIVATION AS REVEALED BY CDK5/P25 AND CDK2/CYCLIN A DYNAMICS" . "11"^^ . . . "B\u00E1rtov\u00E1, Iveta" . "Otyepka, Michal" . "cell cycle; CDK5 regulation; CDK2 regulation; glycine?rich loop; CDK dynamics"@en . "A detailed analysis is presented of the dynamics of human CDK5 in complexes with the protein activator p25 and the purine-like inhibitor roscovitine. These, and other findings related to the activation of CDK5 are critically reviewed from a molecular perspective. In addition, the results obtained on the behavior of CDK5 are compared to data on CDK2 to assess the differences and similarities between the two kinases in terms of (i) roscovitine binding, (ii) regulatory subunit association, (iii) conformational changes in the T-loop following CDK/regulatory subunit complex formation and (iv) specificity in CDK/regulatory subunit recognition. An energy decomposition analysis, used for these purposes, revealed why the binding of p25 alone is sufficient to stabilize the extended active T-loop conformation of CDK5, whereas the equivalent conformational change in CDK2 requires both the binding of Cyclin A and phosphorylation of the Thr160 residue."@en . "281" . . "CZ - \u010Cesk\u00E1 republika" . . . "Ko\u010Da, Jaroslav" . . . . . . "471632" . . "14310" . . "P(GD204/03/H016), P(LC512), Z(MSM0021622413), Z(MSM6198959216)" . "RIV/00216224:14310/06:00015728!RIV10-MSM-14310___" . . "K\u0159\u00ED\u017E, Zden\u011Bk" . . . "[D7FC0243E785]" . "3"^^ . "The Journal of biological chemistry" . . "RIV/00216224:14310/06:00015728" . .