Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme |
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| Authors: | Niefind K Guerra B Ermakowa I Issinger O G |
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| Affiliation: | Universit?t zu K?ln, Institut für Biochemie, Zülpicher Strasse 47, D-50674 K?ln, Germany. Karsten.Niefind@uni-koeln.de |
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| Abstract: | 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. |
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