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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2001-9-14
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pubmed:abstractText |
Surface plasmon resonance analysis shows that the carboxy-terminal domain of Grp94 (Grp94-CT, residues 518-803) physically interacts with the catalytic subunit of protein kinase CK2 (CK2 alpha) under non-stressed conditions. A K(D) of 4 x 10(-7) was determined for this binding. Heparin competed with Grp94-CT for binding to CK2 alpha. CK2 beta also inhibited the binding of Grp94-CT to CK2 alpha, and CK2 holoenzyme reconstituted in vitro was unable to bind Grp94-CT. The use of CK2 alpha mutants made it possible to map the Grp94-CT binding site to the four lysine stretch (residues 74-77) present in helix C of CK2 alpha. Grp94-CT stimulated the activity of CK2 alpha wild-type but was ineffective on the CK2 alpha K74-77A mutant.
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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 |
Sep
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
505
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
42-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11557039-Amino Acid Sequence,
pubmed-meshheading:11557039-Binding Sites,
pubmed-meshheading:11557039-Casein Kinase II,
pubmed-meshheading:11557039-Catalytic Domain,
pubmed-meshheading:11557039-HSP70 Heat-Shock Proteins,
pubmed-meshheading:11557039-Humans,
pubmed-meshheading:11557039-Lysine,
pubmed-meshheading:11557039-Membrane Proteins,
pubmed-meshheading:11557039-Molecular Sequence Data,
pubmed-meshheading:11557039-Mutation,
pubmed-meshheading:11557039-Peptides,
pubmed-meshheading:11557039-Protein Subunits,
pubmed-meshheading:11557039-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11557039-Substrate Specificity,
pubmed-meshheading:11557039-Surface Plasmon Resonance
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pubmed:year |
2001
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pubmed:articleTitle |
The carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme.
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pubmed:affiliation |
Department de Bioquímica i Biologia Molcular, Facultat de Ciències, Universitat Autònoma de Barcelona, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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