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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1988-5-24
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pubmed:abstractText |
Recent molecular cloning experiments have identified a 25 amino-acid region as the calmodulin-binding domain of the alpha-subunit of rat brain Ca2+/calmodulin-dependent multifunctional protein kinase II (CaM-K II). Synthetic peptides, derived from the deduced amino-acid sequence encompassing this region, were examined for their ability to bind calmodulin in a calcium dependent manner and to inhibit the Ca2+/calmodulin-dependent autophosphorylation of CaM-K II. Comparison of these structure-function relationships highlighted a region of 5 amino-acids, which was essential for calmodulin interaction and inhibition of kinase activity. This region demonstrated some homology with other calmodulin-binding peptides, and may represent a key site of interaction of the kinase with calmodulin. These analyses provide additional insight into the molecular mechanism underlying the Ca2+ regulation of CaM-K II.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
152
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
122-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2833884-Amino Acid Sequence,
pubmed-meshheading:2833884-Animals,
pubmed-meshheading:2833884-Binding Sites,
pubmed-meshheading:2833884-Brain,
pubmed-meshheading:2833884-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:2833884-Calmodulin,
pubmed-meshheading:2833884-Kinetics,
pubmed-meshheading:2833884-Peptide Fragments,
pubmed-meshheading:2833884-Phosphorylation,
pubmed-meshheading:2833884-Protein Binding,
pubmed-meshheading:2833884-Protein Kinases,
pubmed-meshheading:2833884-Rats
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pubmed:year |
1988
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pubmed:articleTitle |
Mapping of calmodulin-binding domain of Ca2+/calmodulin-dependent protein kinase II from rat brain.
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pubmed:affiliation |
University of Texas Medical School, Houston.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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