Cyclin-dependent kinase
From Proteopedia
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| - | {{STRUCTURE_3rgf| PDB=3rgf | SIZE= | + | {{STRUCTURE_3rgf| PDB=3rgf | SIZE=350| SCENE= |right|CAPTION=CDK8 (grey) complex with cyclin C (green), sorafenib drug and glycerol (PDB code [[3rgf]]) }} |
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Revision as of 10:18, 16 December 2015
Template:STRUCTURE 3rgf
Cyclin-dependent kinase (CDK) or Cell division protein kinase are serine/threonine kinases which are important to the regulation of the cell cycle. CDKs are small proteins which contain just a kinase domain. In order to function, CDK binds the regulatory protein cyclin. CDKs phosphorylate their substrates at a consensus tetrapeptide. The CDK classes differ by the binding cyclin and their function in human.
• CDK1 binds cyclin and forms a complex which phosphorylates a variety of substrates which are involved in cell cycle progression.
• CDK2 is involved in the control of the cell cycle. It interacts with the regulatory protein cyclin A2. Phosphorylation at Thr14 or Tyr15 inactivates it; phosphorylation at Thr160 (T160P) – activates it. See also Intrinsically Disordered Protein.
• CDK3 binds cyclin C and functions during the G1 phase.
• For details on CDK4 see Cyclin Dependent Kinase-4.
- CDK5 binds p53 and functions during transcription.
• CDK6 binds cyclin D and functions during the G1 phase.
• CDK7 may serve as a direct link between transcription regulation and the cell cycle.
• CDK8 binds cyclin C and functions during transcription.
• CDK12 phosphorylates the C-terminal domain of the large subunit of RNA polymerase II. Acts as a regulator of transcription elongation.
• CDK16 plays a role in vescicle-mdiated transport processes and exocytosis.
3D structures of cyclin-dependent kinase
Updated on 16-December-2015
