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Title
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Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme.
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Authors
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K.Niefind,
B.Guerra,
I.Ermakowa,
O.G.Issinger.
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Ref.
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EMBO J, 2001,
20,
5320-5331.
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PubMed id
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Abstract
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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 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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