Cdk-activating kinase: Difference between revisions
Created page with "The Cdk-activating Kinase (CAK) is a protein belonging to the kinase family of enzymes and plays a vital role in the regulation of the eukaryotic cell cycle. As its name suggests..." |
No edit summary |
||
| Line 1: | Line 1: | ||
The Cdk-activating Kinase (CAK) is a protein belonging to the kinase family of enzymes and plays a vital role in the regulation of the eukaryotic cell cycle. As its name suggests, the CAK performs its function by phosphorylating the Cdk protein (see [ | The Cdk-activating Kinase (CAK) is a protein belonging to the [[kinase|kinase]] family of enzymes and plays a vital role in the regulation of the [[eukaryotic|eukaryotic]] cell cycle. As its name suggests, the CAK performs its function by [[Phosphorylation|phosphorylating]] the Cdk protein (see [[Cylin_dependent_kinases|Cyclin dependent kinases]]), rendering it fully active to perform its respective function in regulating the [[cell cycle|cell cycle]]. Once a Cdk is partially activated by binding to a cyclin [[molecule|molecule]], the CAK phosphorylates a [[threonine|threonine]] residue on a specific part of the Cdk called the T-loop. This T-loop partially blocks the substrate binding site on the Cdk and this phosphorylation causes the T-loop to undergo a small conformational change, revealing the active site and allowing the Cdk to bind to its substrates more efficiently <ref>Alberts, B. Johnson, A. Lewis, J. Raff, M. Roberts, K. and Walter, P. (2008) Molecular Biology of the Cell, 5th Edition, New York: Garland Science</ref>.<br> | ||
=== References === | |||
<references / | <references /> | ||
Latest revision as of 22:21, 27 November 2014
The Cdk-activating Kinase (CAK) is a protein belonging to the kinase family of enzymes and plays a vital role in the regulation of the eukaryotic cell cycle. As its name suggests, the CAK performs its function by phosphorylating the Cdk protein (see Cyclin dependent kinases), rendering it fully active to perform its respective function in regulating the cell cycle. Once a Cdk is partially activated by binding to a cyclin molecule, the CAK phosphorylates a threonine residue on a specific part of the Cdk called the T-loop. This T-loop partially blocks the substrate binding site on the Cdk and this phosphorylation causes the T-loop to undergo a small conformational change, revealing the active site and allowing the Cdk to bind to its substrates more efficiently [1].
References
- ↑ Alberts, B. Johnson, A. Lewis, J. Raff, M. Roberts, K. and Walter, P. (2008) Molecular Biology of the Cell, 5th Edition, New York: Garland Science