pubmed-article:9033593 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9033593 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:9033593 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
pubmed-article:9033593 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:9033593 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
pubmed-article:9033593 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:9033593 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
pubmed-article:9033593 | lifeskim:mentions | umls-concept:C1513371 | lld:lifeskim |
pubmed-article:9033593 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:9033593 | pubmed:dateCreated | 1997-3-20 | lld:pubmed |
pubmed-article:9033593 | pubmed:abstractText | The structure of a complex between the DNA binding domain of the GAGA factor (GAGA-DBD) and an oligonucleotide containing its GAGAG consensus binding site has been determined by nuclear magnetic resonance spectroscopy. The GAGA-DBD comprises a single classical Cys2-His2 zinc finger core, and an N-terminal extension containing two highly basic regions, BR1 and BR2. The zinc finger core binds in the major groove and recognizes the first three GAG bases of the consensus in a manner similar to that seen in other classical zinc finger-DNA complexes. Unlike the latter, which require tandem zinc finger repeats with a minimum of two units for high affinity binding, the GAGA-DBD makes use of only a single finger complemented by BR1 and BR2. BR2 forms a helix that interacts in the major groove recognizing the last G of the consensus, while BR1 wraps around the DNA in the minor groove and recognizes the A in the fourth position of the consensus. The implications of the structure of the GAGA-DBD-DNA complex for chromatin remodelling are discussed. | lld:pubmed |
pubmed-article:9033593 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9033593 | pubmed:language | eng | lld:pubmed |
pubmed-article:9033593 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9033593 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9033593 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9033593 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9033593 | pubmed:month | Feb | lld:pubmed |
pubmed-article:9033593 | pubmed:issn | 1072-8368 | lld:pubmed |
pubmed-article:9033593 | pubmed:author | pubmed-author:FelsenfeldGG | lld:pubmed |
pubmed-article:9033593 | pubmed:author | pubmed-author:CloreG MGM | lld:pubmed |
pubmed-article:9033593 | pubmed:author | pubmed-author:GronenbornA... | lld:pubmed |
pubmed-article:9033593 | pubmed:author | pubmed-author:PedoneP VPV | lld:pubmed |
pubmed-article:9033593 | pubmed:author | pubmed-author:OmichinskiJ... | lld:pubmed |
pubmed-article:9033593 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9033593 | pubmed:volume | 4 | lld:pubmed |
pubmed-article:9033593 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9033593 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9033593 | pubmed:pagination | 122-32 | lld:pubmed |
pubmed-article:9033593 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:9033593 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9033593 | pubmed:articleTitle | The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode. | lld:pubmed |
pubmed-article:9033593 | pubmed:affiliation | Laboratories of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA. | lld:pubmed |
pubmed-article:9033593 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9033593 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
family:PF09237.6 | family:pubmed | pubmed-article:9033593 | lld:pfam |
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