Journal
EMBO JOURNAL
Volume 20, Issue 19, Pages 5320-5331Publisher
WILEY
DOI: 10.1093/emboj/20.19.5320
Keywords
casein kinase 2; CK2 holoenzyme; constitutive activity; protein kinase CK2; X-ray crystallography
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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 Angstrom resolution (Protein Data Bank code: 1JWH). 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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