Eukaryotic elongation factor 2 kinase (eEF2K) is a calcium/calmodulin (Ca2+/CaM)-dependent protein kinase, which phosphorylates and inactivates the translation elongation factor eEF2, thereby slowing down the rate of translation elongation. With Professor Chris Proud and Dr Joern Werner.
The structure and molecular mechanism of regulation of this potential cancer target are not known. The protein consists of an unstructured N-terminal region containing the Ca2+/CaM binding site, a highly atypical α-kinase domain, an unstructured central region with regulatory phosphorylation sites and a structured C-terminal domain containing four Sel1 like repeats. We have taken a divide and conquer approach to study the structure and regulation of this enzyme using a high throughput (HT) parallel cloning and recombinant expression approach for construct screening in conjunction with X-ray crystallography, NMR and ITC.