Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme.
The crystal structure of a fully active form of human protein kinase CK2 (casein kinase 2) consisting of two C-terminally truncated catalytic and two regulatory subunits has been determined at 3.1 A resolution. In the CK2 complex the regulatory subunits form a stable dimer linking the two catalytic subunits, which make no direct contact with one another. Each catalytic subunit interacts with both regulatory chains, predominantly via an extended C-terminal tail of the regulatory subunit. The CK2 structure is consistent with its constitutive activity and with a flexible role of the regulatory subunit as a docking partner for various protein kinases. Furthermore it shows an inter-domain mobility in the catalytic subunit known to be functionally important in protein kinases and detected here for the first time directly within one crystal structure.
Niefind
K
K
Universität zu Köln, Institut für Biochemie, Zülpicher Strasse 47, D-50674 Köln, Germany. Karsten.Niefind@uni-koeln.de
Guerra
B
B
Ermakowa
I
I
Issinger
O G
OG
D000595:Amino Acid Sequence; D047390:Casein Kinase II; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D020035:Holoenzymes / Q000737:chemistry; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009038:Motion; D010446:Peptide Fragments / Q000737:chemistry; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D055672:Static Electricity
D020035:Holoenzymes; D010446:Peptide Fragments; D011994:Recombinant Proteins; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases