The allosteric behavior of kinases consequent to ATP binding was found to be fundamental to the behavior of PKC proteins. This has had implications for the entire kinome including the pseudokinases that retain nucleotide binding properties.

We have established the importance of nucleotide pocket occupation driving conformational change in the PKC family. The generality of this normally ATP-driven behaviour has broad implications for kinases and pseudokinases and has in part explained various anomalous behaviours associated with certain ATP-competitive inhibitors directed at other protein kinases. Conformational switches in kinases consequent to nucleotide binding, suggests that pseudokinases may not be simple 'inert' scaffolds/partners.

Amongst the family of pseudokinases, the EGF receptor family member HER3 is an important regulator in cancer. Work in collaboration with others is addressing the role and mechanisms of HER3 nucleotide pocket occupation (ATP/drug) and the consequent effects of oligomerization, signal output and inhibition.