| pubmed-article:12534274 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12534274 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:12534274 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:12534274 | lifeskim:mentions | umls-concept:C0081594 | lld:lifeskim |
| pubmed-article:12534274 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:12534274 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12534274 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:12534274 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:12534274 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:12534274 | pubmed:dateCreated | 2003-1-21 | lld:pubmed |
| pubmed-article:12534274 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12534274 | pubmed:abstractText | Phosphorylation of some members of the annexin family of proteins may play a significant role in controlling their calcium-dependent interactions with membranes. Recent electron microscopic studies of annexin VI revealed that the protein's two core domains exhibit a great degree of flexibility and are able to undergo a relative conformational change that could potentially initiate contacts between membranes [Avila-Sakar, A. J., et al. (2000) J. Struct. Biol. 130, 54-62]. To assess the possibility of a regulatory role of phosphorylation in this behavior, the crystal structure of a phosphorylation-mimicking mutant (T356D in the flexible connector region of human annexin VI) was determined to 2.65 A resolution. When the mutant is compared to the wild-type annexin VI, subtle differences are seen at the site of the mutation, while larger changes are evident in one of the calcium-binding loops and in the presence of five calcium ions. Furthermore, biochemical studies provide evidence for additional conformational differences between the T356D and wild-type solution structures. Fluorescence emission and acrylamide quenching suggest a higher level of solvent exposure of Trp-343 in the connector region of T356D in the presence of calcium. Comparisons of retardation coefficients in native gel electrophoresis reveal that T356D has a more extended shape, while proteolytic studies show a greater accessibility of a trypsin cleavage site inside the linker region, indicating a conformation more open than the wild-type form. These data provide insights into a possible regulatory mechanism leading to a higher degree of flexibility and possibly a higher calcium binding affinity of annexin VI upon phosphorylation. | lld:pubmed |
| pubmed-article:12534274 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12534274 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12534274 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12534274 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12534274 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12534274 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12534274 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12534274 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12534274 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12534274 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:12534274 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:12534274 | pubmed:author | pubmed-author:KretsingerRob... | lld:pubmed |
| pubmed-article:12534274 | pubmed:author | pubmed-author:CreutzCarl... | lld:pubmed |
| pubmed-article:12534274 | pubmed:author | pubmed-author:Freye-MinksCa... | lld:pubmed |
| pubmed-article:12534274 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12534274 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:12534274 | pubmed:volume | 42 | lld:pubmed |
| pubmed-article:12534274 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12534274 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12534274 | pubmed:pagination | 620-30 | lld:pubmed |
| pubmed-article:12534274 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:12534274 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12534274 | pubmed:articleTitle | Structural and dynamic changes in human annexin VI induced by a phosphorylation-mimicking mutation, T356D. | lld:pubmed |
| pubmed-article:12534274 | pubmed:affiliation | Department of Pharmacology, University of Virginia, Charlottesville, Virginia 22908, USA. cf9c@virginia.edu | lld:pubmed |
| pubmed-article:12534274 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12534274 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12534274 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:309 | entrezgene:pubmed | pubmed-article:12534274 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:12534274 | lld:entrezgene |
