High-resolution crystal structure of cAMP-dependent protein kinase from Cricetulus griseus.

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.

Citation

Denis Kudlinzki, Verena L Linhard, Krishna Saxena, Sridhar Sreeramulu, Santosh Gande, Ulrich Schieborr, Matthias Dreyer, Harald Schwalbe. High-resolution crystal structure of cAMP-dependent protein kinase from Cricetulus griseus. Acta crystallographica. Section F, Structural biology communications. 2015 Aug;71(Pt 8):1088-93

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PMID: 26249705

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