Cyclin-dependent kinase

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PDB ID 3ddq

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CDK8 (grey) complex with cyclin C (green), sorafenib drug and glycerol (PDB code 3rgf)
Ligands: ,
Non-Standard Residues:
Gene: CDK2 (Homo sapiens), CCNA2, CCNA (Bos taurus)
Activity: Cyclin-dependent kinase, with EC number 2.7.11.22
Related: 3ddp
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml


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.[1]

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 vesicle-mediated transport processes and exocytosis.

Relevance

CDK is a potential target for anti-cancer therapy.


3D structures of cyclin-dependent kinase

Updated on 16-December-2015

References

  1. Larsen NA, Turner JM, Stevens J, Rosser SJ, Basran A, Lerner RA, Bruce NC, Wilson IA. Crystal structure of a bacterial cocaine esterase. Nat Struct Biol. 2002 Jan;9(1):17-21. PMID:11742345 doi:10.1038/nsb742

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Michal Harel, Alexander Berchansky

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