| pubmed-article:9582338 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9582338 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:9582338 | lifeskim:mentions | umls-concept:C0070798 | lld:lifeskim |
| pubmed-article:9582338 | lifeskim:mentions | umls-concept:C0250564 | lld:lifeskim |
| pubmed-article:9582338 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9582338 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:9582338 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9582338 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:9582338 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:9582338 | pubmed:dateCreated | 1998-6-25 | lld:pubmed |
| pubmed-article:9582338 | pubmed:abstractText | Syndecan-4, a transmembrane heparan sulfate proteoglycan, is a coreceptor with integrins in cell adhesion. It has been suggested to form a ternary signaling complex with protein kinase Calpha and phosphatidylinositol 4,5-bisphosphate (PIP2). Syndecans each have a unique, central, and variable (V) region in their cytoplasmic domains, and that of syndecan-4 is critical to its interaction with protein kinase C and PIP2. Two oligopeptides corresponding to the variable region (4V) and whole domain (4L) of syndecan-4 cytoplasmic domain were synthesized for nuclear magnetic resonance (NMR) studies. Data from NMR and circular dichroism indicate that the cytoplasmic domain undergoes a conformational transition and forms a symmetric dimer in the presence of phospholipid activator PIP2. The solution conformations of both free and PIP2-complexed 4V have been determined by two-dimensional NMR spectroscopy and dynamical simulated annealing calculations. The 4V peptide in the presence of PIP2 formed a compact dimer with two twisted strands packed parallel to each other and the exposed surface of the dimer consisted of highly charged and polar residues. The overall three-dimensional structure in solution exhibits a twisted clamp shape having a cavity in the center of dimeric interface. In addition, it has been observed that the syndecan-4V strongly interacts not only with fatty acyl groups but also the anionic head group of PIP2. These findings reveal that PIP2 promotes oligomerization of syndecan-4 cytoplasmic domain for transmembrane signaling and cell-matrix adhesion. | lld:pubmed |
| pubmed-article:9582338 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582338 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9582338 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582338 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9582338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9582338 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582338 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9582338 | pubmed:month | May | lld:pubmed |
| pubmed-article:9582338 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9582338 | pubmed:author | pubmed-author:LebAA | lld:pubmed |
| pubmed-article:9582338 | pubmed:author | pubmed-author:LeaSS | lld:pubmed |
| pubmed-article:9582338 | pubmed:author | pubmed-author:WoodsAA | lld:pubmed |
| pubmed-article:9582338 | pubmed:author | pubmed-author:CouchmanJ RJR | lld:pubmed |
| pubmed-article:9582338 | pubmed:author | pubmed-author:OhE SES | lld:pubmed |
| pubmed-article:9582338 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9582338 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:9582338 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9582338 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9582338 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9582338 | pubmed:pagination | 13022-9 | lld:pubmed |
| pubmed-article:9582338 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9582338 | pubmed:meshHeading | pubmed-meshheading:9582338-... | lld:pubmed |
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| pubmed-article:9582338 | pubmed:meshHeading | pubmed-meshheading:9582338-... | lld:pubmed |
| pubmed-article:9582338 | pubmed:meshHeading | pubmed-meshheading:9582338-... | lld:pubmed |
| pubmed-article:9582338 | pubmed:meshHeading | pubmed-meshheading:9582338-... | lld:pubmed |
| pubmed-article:9582338 | pubmed:meshHeading | pubmed-meshheading:9582338-... | lld:pubmed |
| pubmed-article:9582338 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9582338 | pubmed:articleTitle | Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate. | lld:pubmed |
| pubmed-article:9582338 | pubmed:affiliation | Department of Biochemistry, College of Science, Yonsei University, Seoul 120-740, Korea. | lld:pubmed |
| pubmed-article:9582338 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9582338 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9582338 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:6385 | entrezgene:pubmed | pubmed-article:9582338 | lld:entrezgene |
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