High-resolution crystal structure of cAMP-dependent protein kinase fromCricetulus griseus
D. Kudlinzki, V.L. Linhard, Krishna Saxena, Sridhar Sreeramulu, S.L. Gande, Ulrich Schieborr, Matthias Dreyer, Harald Schwalbe · Acta Crystallographica Section F Structural Biology Communications · 2015
Protein kinases (PKs) are dynamic regulators of numerous cellular processes. Their phosphorylation activity is determined by the conserved kinase core structure, which is maintained by the interaction and dynamics with associated domains or interacting proteins. The prototype enzyme for investigations to understand the activity and regulation of PKs is the catalytic subunit of cAMP-dependent protein kinase (PKAc). Major effects of functional regulation and ligand binding are driven by only minor structural modulations in protein-protein interactions. In order to resolve such minor structural differences, very high resolution structures are required. Here, the high-resolution X-ray structure of PKAc from Cricetulus griseus is reported.