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Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme.

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.

SUBMITTER: Niefind K

PROVIDER: S-EPMC125641 | biostudies-literature | 2001 Oct

REPOSITORIES: biostudies-literature

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Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme.

Niefind K K Guerra B B Ermakowa I I Issinger O G OG

The EMBO journal 20011001 19

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 ...[more]

PMID: 11574463

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