Protein kinases achieve substrate selective phosphorylation through their conformational
flexibility and dynamic interaction with the substrate. Designing substrate selective or kinase …

Protein kinases have emerged as the largest family of signaling proteins in eukaryotic cells
and are involved in every aspect of cellular regulation. There are over 500 protein kinases in …

Conformational changes of catalytically-important structural elements are a key feature of
the regulation mechanisms of protein kinases and are important for dictating inhibitor …

ATP-competitive inhibitors that demonstrate exquisite selectivity for specific members of the
human kinome have been developed. Despite this success, the identification of highly …

There is significant interest in identifying and characterizing allosteric sites in enzymes such
as protein kinases both for understanding allosteric mechanisms as well as for drug …

Multidomain protein kinases, central controllers of signal transduction, use regulatory
domains to modulate catalytic activity in a complex cellular environment. Additionally, these …

Protein–protein interactions often regulate the activity of protein kinases by allosterically
modulating the conformation of the ATP-binding site. Bidirectional allostery implies that …

Protein kinases use ATP to phosphorylate other proteins. Phosphorylation (p) universally
orchestrates a fine-tuned network modulating a multitude of biological processes. Moreover …

Protein kinases are key components in cellular signaling pathways as they carry out the
phosphorylation of proteins, primarily on Ser, Thr, and Tyr residues. The catalytic activity of …

Signal transduction pathways use protein kinases for the modification of protein function by
phosphorylation. A major question in the field is how protein kinases achieve the specificity …