Protein kinase: Difference between revisions

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<gallery>
File:Kinase_function.png|Protein kinase function
File:Inorganic-phosphate-3D-balls.png|Inorganic phosphate 3D model
File:CaMKII.png|CaMKII structure
</gallery>

Latest revision as of 02:13, 18 February 2025

Protein Kinase

A Protein kinase is a type of enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation). This process is a crucial aspect of cell signaling and regulates cellular activities such as protein-protein interaction and protein degradation.

Function[edit]

Protein kinases play a pivotal role in the regulation of many cellular processes including cell cycle, gene expression, and differentiation. They can become overactive or inactive in many types of cancer, and a number of inhibitors have been developed to control them.

Classification[edit]

Protein kinases are classified into broad groups by the substrate they act on: serine/threonine-specific protein kinases, tyrosine kinases, and dual-specificity kinases. They can also be categorized by their function within the signal transduction pathways.

Structure[edit]

The structure of protein kinases is largely conserved, with a small, generally N-terminal, lobe that binds adenosine triphosphate (ATP) and a large C-terminal lobe that binds the protein substrate. The two lobes are linked by a hinge region that aligns the lobes in the correct orientation.

Clinical significance[edit]

Protein kinases have been identified as a cause of several diseases, such as cancer, inflammation, and neurodegenerative diseases. They are also the target of a number of pharmaceuticals, which inhibit their activity.

See also[edit]

References[edit]

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