| pubmed-article:8784353 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8784353 | lifeskim:mentions | umls-concept:C0031671 | lld:lifeskim |
| pubmed-article:8784353 | lifeskim:mentions | umls-concept:C1511359 | lld:lifeskim |
| pubmed-article:8784353 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:8784353 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:8784353 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:8784353 | pubmed:dateCreated | 1996-10-15 | lld:pubmed |
| pubmed-article:8784353 | pubmed:abstractText | The structure of the PH-domain truncated core of rat phosphoinositide-specific phospholipase C-delta 1 has been determined at 2.4 A resolution and compared to the structure previously determined in a different crystal form. The stereochemical relationship between the EF, catalytic, and C2 domains is essentially identical. The Ca2+ analogue Sm3+ binds at two sites between the jaws of the C2 domain. Sm3+ binding ejects three lysine residues which bridge the gap between the jaws and occupy the Ca2+ site in the apoenzyme, triggering a conformational change in the jaws. The distal sections of the C2 jaws move apart, opening the mouth by 9 A and creating a gap large enough to bind a phospholipid headgroup. | lld:pubmed |
| pubmed-article:8784353 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8784353 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8784353 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8784353 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8784353 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8784353 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8784353 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8784353 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8784353 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8784353 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8784353 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:8784353 | pubmed:author | pubmed-author:WilliamsR LRL | lld:pubmed |
| pubmed-article:8784353 | pubmed:author | pubmed-author:EssenL OLO | lld:pubmed |
| pubmed-article:8784353 | pubmed:author | pubmed-author:HurleyJ HJH | lld:pubmed |
| pubmed-article:8784353 | pubmed:author | pubmed-author:GroblerJ AJA | lld:pubmed |
| pubmed-article:8784353 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8784353 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:8784353 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8784353 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8784353 | pubmed:pagination | 788-95 | lld:pubmed |
| pubmed-article:8784353 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:8784353 | pubmed:meshHeading | pubmed-meshheading:8784353-... | lld:pubmed |
| pubmed-article:8784353 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8784353 | pubmed:articleTitle | C2 domain conformational changes in phospholipase C-delta 1. | lld:pubmed |
| pubmed-article:8784353 | pubmed:affiliation | Laboratory of Molecular Biology, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0580, USA. | lld:pubmed |
| pubmed-article:8784353 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8784353 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:24655 | entrezgene:pubmed | pubmed-article:8784353 | lld:entrezgene |
| family:PF09279.6 | family:pubmed | pubmed-article:8784353 | lld:pfam |
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