| pubmed-article:15050832 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15050832 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:15050832 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:15050832 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:15050832 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:15050832 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:15050832 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:15050832 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15050832 | pubmed:dateCreated | 2004-3-30 | lld:pubmed |
| pubmed-article:15050832 | pubmed:abstractText | pp60v-src tyrosine protein kinase was suggested to interact with Ca2+-bound calmodulin (Ca2+/CaM) through the N-terminal region based on its structural similarities to CAP-23/NAP-22, a myristoylated neuron-specific protein, whose myristoyl group is essential for interaction with Ca2+/CaM; (1) the N terminus of pp60v-src is myristoylated like CAP-23/NAP-22; (2) both lysine residues are required for the myristoylation-dependent interaction and serine residues that are thought to regulate the interaction through the phosphorylations located in the N-terminal region of pp60v-src. To verify this possibility, we investigated the direct interaction between pp60v-src and Ca2+/CaM using a myristoylated peptide corresponding to the N-terminal region of pp60v-src. The binding assay indicated that only the myristoylated peptide binds to Ca2+/CaM, and the non-myristoylated peptide is not able to bind to Ca2+/CaM. Analyses of the binding kinetics revealed two independent reactions with the dissociation constants (KD) of 2.07 x 10(-9)M (KD1) and 3.93 x 10(-6)M (KD2), respectively. Two serine residues near the myristoyl moiety of the peptide (Ser2, Ser11) were phosphorylated by protein kinase C in vitro, and the phosphorylation drastically reduced the interaction. NMR experiments indicated that two molecules of the myristoylated peptide were bound around the hydrophobic clefts of a Ca2+/CaM molecule. The small-angle X-ray scattering analyses showed that the size of the peptide-Ca2+/CaM complex is 2-3A smaller than that of the known Ca2+/CaM-target molecule complexes. These results demonstrate clearly the direct interaction between pp60v-src and Ca2+/CaM in a novel manner different from that of known Ca2+/CaM, the target molecules, interactions. | lld:pubmed |
| pubmed-article:15050832 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15050832 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15050832 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15050832 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15050832 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15050832 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15050832 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15050832 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15050832 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15050832 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15050832 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15050832 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:15050832 | pubmed:author | pubmed-author:ItoYutakaY | lld:pubmed |
| pubmed-article:15050832 | pubmed:author | pubmed-author:HashimotoKeii... | lld:pubmed |
| pubmed-article:15050832 | pubmed:author | pubmed-author:TitaniKoitiK | lld:pubmed |
| pubmed-article:15050832 | pubmed:author | pubmed-author:HayashiNobuhi... | lld:pubmed |
| pubmed-article:15050832 | pubmed:author | pubmed-author:JinboYujiY | lld:pubmed |
| pubmed-article:15050832 | pubmed:author | pubmed-author:IzumiYoshinob... | lld:pubmed |
| pubmed-article:15050832 | pubmed:author | pubmed-author:MatsushimaNor... | lld:pubmed |
| pubmed-article:15050832 | pubmed:author | pubmed-author:YamakawaYoshi... | lld:pubmed |
| pubmed-article:15050832 | pubmed:author | pubmed-author:TakasakiAkihi... | lld:pubmed |
| pubmed-article:15050832 | pubmed:author | pubmed-author:NakagawaChisa... | lld:pubmed |
| pubmed-article:15050832 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15050832 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:15050832 | pubmed:volume | 338 | lld:pubmed |
| pubmed-article:15050832 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15050832 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15050832 | pubmed:pagination | 169-80 | lld:pubmed |
| pubmed-article:15050832 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:15050832 | pubmed:meshHeading | pubmed-meshheading:15050832... | lld:pubmed |
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| pubmed-article:15050832 | pubmed:meshHeading | pubmed-meshheading:15050832... | lld:pubmed |
| pubmed-article:15050832 | pubmed:meshHeading | pubmed-meshheading:15050832... | lld:pubmed |
| pubmed-article:15050832 | pubmed:meshHeading | pubmed-meshheading:15050832... | lld:pubmed |
| pubmed-article:15050832 | pubmed:meshHeading | pubmed-meshheading:15050832... | lld:pubmed |
| pubmed-article:15050832 | pubmed:meshHeading | pubmed-meshheading:15050832... | lld:pubmed |
| pubmed-article:15050832 | pubmed:meshHeading | pubmed-meshheading:15050832... | lld:pubmed |
| pubmed-article:15050832 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15050832 | pubmed:articleTitle | Myristoylation-regulated direct interaction between calcium-bound calmodulin and N-terminal region of pp60v-src. | lld:pubmed |
| pubmed-article:15050832 | pubmed:affiliation | Division of Biomedical Polymer Science, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi 470-1192, Japan. nhayashi@fujita-hu.ac.jp | lld:pubmed |
| pubmed-article:15050832 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15050832 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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