An Overview of Protein Kinase Inhibitors

Protein kinases become one of the most successful drug targets for the treatment of various diseases. Protein kinase catalyzes the transfer of the γ-phosphoryl group of the ATP to specific protein substrates which is an important cellular signal communication and maintenance of homeostasis. Most kinases share a common protein kinase domain. Some kinase inhibitors bind to the ATP site and some inhibitors bind to the allosteric site. There are 82 kinase inhibitors in the market. Here chemical structures of approved kinase inhibitors, their binding modes, medical uses, and names of drug developers are described. Humans have four typical MAP kinases such as extracellular signal-regulated kinases (ERKs), c-Jun N-terminal kinases (JNKs), p38 MAP kinases, and nemo-like kinase (NLK), and their structure and activation, cellular signaling, and pathological implications are highlighted.