Protein kinases

Protein kinases are a group of enzymes that modify other proteins by chemically adding phosphate groups to them (phosphorylation). This process is a crucial aspect of cell signaling and regulates many cellular processes, including metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation.

Structure

Protein kinases have a common structural framework that is conserved from yeast to humans. The structure is typically a two-lobed, heart-shaped molecule. The smaller lobe, the N-terminal lobe, primarily consists of beta sheets. The larger lobe, the C-terminal lobe, is mostly alpha helical. The two lobes are linked by a hinge region that forms the peptide-binding site.

Function

Protein kinases function by phosphorylating other proteins, a process that changes the function of the phosphorylated protein. This can result in a wide range of effects, including changes in cell shape, movement, division, and death. Protein kinases are involved in the regulation of most cellular pathways, especially those involved in signal transduction.

Classification

Protein kinases can be classified into several categories based on their structure, function, and the substrates they act on. The two main groups are the serine/threonine kinases and the tyrosine kinases. There are also many other types of protein kinases, including histidine kinases, aspartate kinases, and dual-specificity kinases.

Clinical significance

Protein kinases are important targets for drug development, as they play key roles in many diseases, including cancer, diabetes, and inflammatory diseases. Many drugs that target protein kinases have been developed and are in use in the clinic, including imatinib, erlotinib, and sunitinib.

See also

• Kinase
• Phosphorylation
• Signal transduction
• Enzyme

Protein kinases Resources
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