| pubmed-article:10562559 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10562559 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:10562559 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:10562559 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:10562559 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:10562559 | pubmed:dateCreated | 2000-1-20 | lld:pubmed |
| pubmed-article:10562559 | pubmed:abstractText | The hinge-region of the lac repressor plays an important role in the models for induction and DNA looping in the lac operon. When lac repressor is bound to a tight-binding symmetric operator, this region forms an alpha-helix that induces bending of the operator. The presence of the hinge-helices is questioned by previous data that suggest that the repressor does not bend the wild-type operator. We show that in the wild-type complex the hinge-helices are formed and the DNA is bent, similar to the symmetric complex. Furthermore, our data show differences in the binding of the DNA binding domains to the half-sites of the wild-type operator and reveal the role of the central base-pair of the wild-type operator in the repressor-operator interaction. The differences in binding to the operator half-sites are incorporated into a model that explains the relative affinities of the repressor for various lac operator sequences that contain left and right half-sites with different spacer lengths. | lld:pubmed |
| pubmed-article:10562559 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10562559 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10562559 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10562559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10562559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10562559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10562559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10562559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10562559 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10562559 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:10562559 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:10562559 | pubmed:author | pubmed-author:KapteinRR | lld:pubmed |
| pubmed-article:10562559 | pubmed:author | pubmed-author:BoelensRR | lld:pubmed |
| pubmed-article:10562559 | pubmed:author | pubmed-author:FolkersG EGE | lld:pubmed |
| pubmed-article:10562559 | pubmed:author | pubmed-author:SpronkC ACA | lld:pubmed |
| pubmed-article:10562559 | pubmed:author | pubmed-author:Wechselberger... | lld:pubmed |
| pubmed-article:10562559 | pubmed:author | pubmed-author:NoordmanA MAM | lld:pubmed |
| pubmed-article:10562559 | pubmed:author | pubmed-author:van den... | lld:pubmed |
| pubmed-article:10562559 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10562559 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10562559 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:10562559 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10562559 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10562559 | pubmed:pagination | 6472-80 | lld:pubmed |
| pubmed-article:10562559 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:10562559 | pubmed:meshHeading | pubmed-meshheading:10562559... | lld:pubmed |
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| pubmed-article:10562559 | pubmed:meshHeading | pubmed-meshheading:10562559... | lld:pubmed |
| pubmed-article:10562559 | pubmed:meshHeading | pubmed-meshheading:10562559... | lld:pubmed |
| pubmed-article:10562559 | pubmed:meshHeading | pubmed-meshheading:10562559... | lld:pubmed |
| pubmed-article:10562559 | pubmed:meshHeading | pubmed-meshheading:10562559... | lld:pubmed |
| pubmed-article:10562559 | pubmed:meshHeading | pubmed-meshheading:10562559... | lld:pubmed |
| pubmed-article:10562559 | pubmed:meshHeading | pubmed-meshheading:10562559... | lld:pubmed |
| pubmed-article:10562559 | pubmed:meshHeading | pubmed-meshheading:10562559... | lld:pubmed |
| pubmed-article:10562559 | pubmed:meshHeading | pubmed-meshheading:10562559... | lld:pubmed |
| pubmed-article:10562559 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10562559 | pubmed:articleTitle | Hinge-helix formation and DNA bending in various lac repressor-operator complexes. | lld:pubmed |
| pubmed-article:10562559 | pubmed:affiliation | Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. | lld:pubmed |
| pubmed-article:10562559 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10562559 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:945007 | entrezgene:pubmed | pubmed-article:10562559 | lld:entrezgene |
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