Protein-protein interactions in the allosteric regulation of protein kinases

Protein-protein interactions involving the catalytic domain of protein kinases are likely to be generally important in the regulation of signal transduction pathways, but are rather sparsely represented in crystal structures. Recently determined structures of the kinase domains of the mitogena-ctivated protein kinase Fus3, the RNA-dependent kinase PKR, the epidermal growth factor receptor and Ca2+/ calmodulin-dependent protein kinase II have revealed unexpected and distinct mechanisms by which interactions with the catalytic domain can modulate kinase activity.