4WIH

Crystal structure of cAMP-dependent Protein Kinase A from Cricetulus griseus

Summary for 4WIH

• Entry DOI: 10.2210/pdb4wih/pdb
• Descriptor: cAMP-dependent protein kinase catalytic subunit alpha, cAMP Dependent Protein Kinase Inhibitor PKI-tide (3 entities in total)
• Functional Keywords: pka, kinase, serine/threonine-protein kinase, transferase, atp-binding, camp, nucleotide-binding
• Biological source: Cricetulus griseus (Chinese hamster); More
• Cellular location: Cytoplasm : P25321
• Total number of polymer chains: 2
• Total formula weight: 43107.08

Authors

Kudlinzki, D.,Linhard, V.L.,Saxena, K.,Dreyer, M.,Schwalbe, H. (deposition date: 2014-09-25, release date: 2014-10-22, Last modification date: 2024-11-06)

Primary citation

Kudlinzki, D.,Linhard, V.L.,Saxena, K.,Sreeramulu, S.,Gande, S.,Schieborr, U.,Dreyer, M.,Schwalbe, H.
High-resolution crystal structure of cAMP-dependent protein kinase from Cricetulus griseus.
Acta Crystallogr.,Sect.F, 71:1088-1093, 2015

PubMed Abstract: 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.

PubMed: 26249705
DOI: 10.1107/S2053230X1501242X

Experimental method

X-RAY DIFFRACTION (1.139 Å)