Protein Kinase: Structure, Function and Inhibitors
A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".
Deadline for manuscript submissions: 31 May 2026 | Viewed by 1
Special Issue Editor
Special Issue Information
Dear Colleagues,
Protein kinases are essential components of cellular signaling pathways, mediating protein phosphorylation mainly at serine, threonine, and tyrosine residues. They act as dynamic molecular switches influenced by protein–protein interactions and post-translational modifications, which coordinate essential signal transduction processes such as cell cycle regulation and organismal development. Malfunctioning protein kinases have been recognized as a common cause of various diseases, including cancer, inflammation, infections, and neurodegenerative disorders. As a result, the development of kinase inhibitors has become a prominent focus in drug discovery over the past decades, and high-throughput efforts in structure determination have generated substantial reserves of structural and chemogenomic data to aid the development of kinase inhibitors. This molecular insight has been essential for oncology drug discovery, enabling the development of highly effective anticancer therapies. Furthermore, growing knowledge of allosteric regulation has driven efforts to design both conventional targeted inhibitors and allosteric modulators, particularly to address mutant kinases implicated in cancer. Amid the complexity of regulatory mechanisms governing kinase activity, dimerization-driven activation also emerges as a key allosteric process conserved across multiple kinase families. Recent advances in structural biology, genetics, and pharmacology have substantially deepened our understanding of kinase activation mechanisms, ligand binding dynamics, and allosteric regulation critical for signal propagation.
Prof. Dr. José Bubis
Guest Editor
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Keywords
- protein kinase
- protein phosphorylation
- ATP-binding site
- allosteric regulation
- structure–function relationship
- conformational change
- cellular signaling pathways
- drug discovery
- ATP-competitive inhibitors
- allosteric inhibitors
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