Cdk activity is regulated in several ways. Sort each of the following forms of Cdk into the active or inactive Cdk category. Items (5 items) (Drag and drop into the appropriate area below) Tloop in active site Cdk/cyclin bound to p27 Threonine in T loop phosphorylated Cdk bound to cyclin Cdk alone Categories Active Cdk Inactive Cdk Drag and drop here Drag and drop here

CD kinase is a subtype of kinase enzyme involved in the cell cycle, DNA and mRNA transcription. CDK triggers the phosphorylation of serine and threonine amino acid residues called serine kinases. Cyclin is a CDK activator that forms a CDK complex with the CDK catalytic subunit.

CDK regulation largely occurs through the control of cyclin production and degradation, as cyclin binding shifts the T-loop, exposing substrate-binding sites and aligning critical residues in the active site that prime the kinase to activate.

In resting cells, CDK4/6 and CDK2 are inactive. D-type cyclin levels are low due to a lack of mitogenic stimulus, limiting CDK4/6 activity. In addition, CDK 4 and 6 are bound by members of the INK4 family, forming binary complexes that lack kinase activity. The CDK2 complex is inhibited by the CIP/KIP proteins p21 and p27.

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