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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
2001-9-27
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11574463-10094395,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/11574463-9877159
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5320-31
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11574463-Amino Acid Sequence,
pubmed-meshheading:11574463-Casein Kinase II,
pubmed-meshheading:11574463-Catalytic Domain,
pubmed-meshheading:11574463-Crystallography, X-Ray,
pubmed-meshheading:11574463-Holoenzymes,
pubmed-meshheading:11574463-Humans,
pubmed-meshheading:11574463-Models, Molecular,
pubmed-meshheading:11574463-Molecular Sequence Data,
pubmed-meshheading:11574463-Motion,
pubmed-meshheading:11574463-Peptide Fragments,
pubmed-meshheading:11574463-Protein Structure, Tertiary,
pubmed-meshheading:11574463-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11574463-Recombinant Proteins,
pubmed-meshheading:11574463-Static Electricity
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pubmed:year |
2001
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pubmed:articleTitle |
Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme.
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pubmed:affiliation |
Universität zu Köln, Institut für Biochemie, Zülpicher Strasse 47, D-50674 Köln, Germany. Karsten.Niefind@uni-koeln.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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