| pubmed-article:7947760 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7947760 | lifeskim:mentions | umls-concept:C0442504 | lld:lifeskim |
| pubmed-article:7947760 | lifeskim:mentions | umls-concept:C0812201 | lld:lifeskim |
| pubmed-article:7947760 | lifeskim:mentions | umls-concept:C0162807 | lld:lifeskim |
| pubmed-article:7947760 | lifeskim:mentions | umls-concept:C0012940 | lld:lifeskim |
| pubmed-article:7947760 | lifeskim:mentions | umls-concept:C0282642 | lld:lifeskim |
| pubmed-article:7947760 | lifeskim:mentions | umls-concept:C1512142 | lld:lifeskim |
| pubmed-article:7947760 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
| pubmed-article:7947760 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:7947760 | pubmed:issue | 46 | lld:pubmed |
| pubmed-article:7947760 | pubmed:dateCreated | 1994-12-21 | lld:pubmed |
| pubmed-article:7947760 | pubmed:abstractText | The members of the ets gene family of transcription factors are characterized by a conserved 85-residue DNA-binding region, termed the ETS domain, that lacks sequence homology to structurally characterized DNA-binding motifs. The secondary structure of the ETS domain of murine Ets-1 was determined on the basis of NMR chemical shifts, NOE and J-coupling constraints, amide hydrogen exchange, circular dichroism, and FT-IR spectroscopy. The ETS domain is composed of three alpha-helices (H) and four beta-strands (S) arranged in the order H1-S1-S2-H2-H3-S3-S4. The four-stranded antiparallel beta-sheet is the scaffold for a putative helix-turn-helix DNA recognition motif formed by helices 2 and 3. The 25 residues extending beyond the ETS domain to the native C-terminus of the truncated Ets-1 also contain a helical segment. On the basis of the similarity of this topology with that of catabolite activator protein (CAP), heat shock factor (HSF), and hepatocyte nuclear factor (HNF-3 gamma), we propose that ets proteins are members of the superfamily of winged helix-turn-helix DNA-binding proteins. | lld:pubmed |
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| pubmed-article:7947760 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7947760 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7947760 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7947760 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7947760 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:7947760 | pubmed:author | pubmed-author:GravesB JBJ | lld:pubmed |
| pubmed-article:7947760 | pubmed:author | pubmed-author:PetersenJ MJM | lld:pubmed |
| pubmed-article:7947760 | pubmed:author | pubmed-author:McIntoshL PLP | lld:pubmed |
| pubmed-article:7947760 | pubmed:author | pubmed-author:DonaldsonL... | lld:pubmed |
| pubmed-article:7947760 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7947760 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:7947760 | pubmed:volume | 33 | lld:pubmed |
| pubmed-article:7947760 | pubmed:geneSymbol | ets | lld:pubmed |
| pubmed-article:7947760 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7947760 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7947760 | pubmed:pagination | 13509-16 | lld:pubmed |
| pubmed-article:7947760 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7947760 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7947760 | pubmed:articleTitle | Secondary structure of the ETS domain places murine Ets-1 in the superfamily of winged helix-turn-helix DNA-binding proteins. | lld:pubmed |
| pubmed-article:7947760 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada. | lld:pubmed |
| pubmed-article:7947760 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7947760 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7947760 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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