pubmed-article:9533689 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9533689 | lifeskim:mentions | umls-concept:C1622186 | lld:lifeskim |
pubmed-article:9533689 | lifeskim:mentions | umls-concept:C0061187 | lld:lifeskim |
pubmed-article:9533689 | lifeskim:mentions | umls-concept:C0680730 | lld:lifeskim |
pubmed-article:9533689 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
pubmed-article:9533689 | lifeskim:mentions | umls-concept:C1148554 | lld:lifeskim |
pubmed-article:9533689 | lifeskim:mentions | umls-concept:C0302167 | lld:lifeskim |
pubmed-article:9533689 | pubmed:issue | 2 Pt 1 | lld:pubmed |
pubmed-article:9533689 | pubmed:dateCreated | 1998-5-22 | lld:pubmed |
pubmed-article:9533689 | pubmed:abstractText | Gelsolin is a six-domain protein that regulates actin assembly by severing, capping, and nucleating filaments. We have used electron cryomicroscopy and helical reconstruction to identify its binding site on F-actin. To obtain fully decorated filaments under severing conditions, we have studied a derivative (G2-6) that has a reduced severing efficiency compared to gelsolin. A three-dimensional reconstruction of G2-6:F-actin was obtained by electron cryomicroscopy and helical reconstruction. The structure shows that gelsolin bridges two longitudinally associated monomers when it binds the filament. The F-actin binding region of G2-6 is centered axially at subdomain 3 and radially between subdomains 1 and 3 of the upper actin monomer. Our results suggest that for severing to occur, both gelsolin and actin undergo large conformational changes. | lld:pubmed |
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pubmed-article:9533689 | pubmed:language | eng | lld:pubmed |
pubmed-article:9533689 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9533689 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9533689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9533689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9533689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9533689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9533689 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9533689 | pubmed:month | Feb | lld:pubmed |
pubmed-article:9533689 | pubmed:issn | 0006-3495 | lld:pubmed |
pubmed-article:9533689 | pubmed:author | pubmed-author:ChinLL | lld:pubmed |
pubmed-article:9533689 | pubmed:author | pubmed-author:WayMM | lld:pubmed |
pubmed-article:9533689 | pubmed:author | pubmed-author:McGoughAA | lld:pubmed |
pubmed-article:9533689 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9533689 | pubmed:volume | 74 | lld:pubmed |
pubmed-article:9533689 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9533689 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9533689 | pubmed:pagination | 764-72 | lld:pubmed |
pubmed-article:9533689 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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