Protein kinase R (PKR) is a key signalling molecule implicated in resistance to virus infection, inflammation
and cancer. PKR is activated by external stress stimuli and undergoes autophosphorylation, regulating its
ability to phosphorylate downstream substrates. We aim to measure the biological consequence of key
structural and phospho-residues in PKR-mediated cellular responses, by generating a detailed
phosphorylation map of PKR and defining the ternary structure of the kinase to place phosphorylated
residues in the context of protein function. These outcomes will be significant in understanding the function of
PKR, and will advance our ability to control immune responses.