Cyclin-dependent kinase
From Proteopedia
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| - | {{ | + | {{STRUCTURE_3ddq| PDB=3ddq | SIZE=350| SCENE= |right|CAPTION=CDK8 (grey) complex with cyclin C (green), sorafenib drug and glycerol (PDB code [[3rgf]]) }} |
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| - | '''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.<br /> | + | '''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.<ref>PMID:11742345</ref><br /> |
• '''CDK1''' binds cyclin and forms a complex which phosphorylates a variety of substrates which are involved in cell cycle progression. <br /> | • '''CDK1''' binds cyclin and forms a complex which phosphorylates a variety of substrates which are involved in cell cycle progression. <br /> | ||
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• '''CDK8''' binds cyclin C and functions during transcription.<br /> | • '''CDK8''' binds cyclin C and functions during transcription.<br /> | ||
• '''CDK12''' phosphorylates the C-terminal domain of the large subunit of RNA polymerase II. Acts as a regulator of transcription elongation.<br /> | • '''CDK12''' phosphorylates the C-terminal domain of the large subunit of RNA polymerase II. Acts as a regulator of transcription elongation.<br /> | ||
| - | • '''CDK16''' plays a role in | + | • '''CDK16''' plays a role in vesicle-mediated transport processes and exocytosis. |
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| + | == Relevance == | ||
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| + | CDK is a potential target for anti-cancer therapy. | ||
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==3D structures of cyclin-dependent kinase== | ==3D structures of cyclin-dependent kinase== | ||
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**[[3mtl]] – hCDK16 (mutant) + indirubin<br /> | **[[3mtl]] – hCDK16 (mutant) + indirubin<br /> | ||
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| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:53, 16 December 2015
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
- ↑ 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
