CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes

Full activity of most CDKs is dependent on CAK mediated phosphorylation at a conserved residue (Thr161 in Cdc2). This modification is thought to improve substrate binding. Cyclin B:Cdc2 complexes have considerably low activity in the absence of CAK mediated phosphorylation (Desai et al 1995).

大多数细胞周期调控因子（CDKs）的全面活性依赖于CAK介导的磷酸化作用，这一作用发生在保守的残基（Cdc2中的Thr161）上。此修饰作用被认为可增强底物结合。在缺乏CAK介导的磷酸化作用的情况下，Cyclin B:Cdc2复合物活性显著降低（Desai等，1995年）。