| pubmed-article:8383553 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8383553 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8383553 | lifeskim:mentions | umls-concept:C0140280 | lld:lifeskim |
| pubmed-article:8383553 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8383553 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8383553 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:8383553 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8383553 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:8383553 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8383553 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8383553 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8383553 | pubmed:dateCreated | 1993-4-13 | lld:pubmed |
| pubmed-article:8383553 | pubmed:abstractText | The three-dimensional structure of the DNA-binding domain of the human retinoic acid receptor-beta (hRAR-beta) has been determined by nuclear magnetic resonance spectroscopy in conjunction with distance geometry, restrained molecular dynamics and iterative relaxation matrix calculations. A total of 1244 distance restraints were obtained from NOE intensities, of which 448 were intra-residue and 796 inter-residue restraints. In addition 23 chi and 30 phi dihedral angle restraints were obtained from J-coupling data. The two 'zinc-finger' regions of the 80-amino acid residue protein are followed by two alpha-helices that cross each other perpendicularly. There is a short stretch of b-sheet near the N-terminus. The alpha-helical core of the protein is well determined with a backbone root-mean-square deviation (r.m.s.d.) with respect to the average of 0.18 A and 0.37 A when the side chains of residues 31, 32, 36, 61, 62, 65 and 69 are included. The r.m.s.d. for the backbone of residues 5-80 is 0.76 A. For the first finger (residues 8-28), the r.m.s.d. of the backbone is 0.79 A. For the second finger (residues 44-62) the r.m.s.d. is 0.64 A. The overall structure is similar to that of the corresponding domain of the glucocorticoid receptor, although the C-terminal part of the protein is different. The second alpha-helix is two residues shorter and is followed by a well-defined region of extended backbone structure. | lld:pubmed |
| pubmed-article:8383553 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8383553 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8383553 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8383553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8383553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8383553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8383553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8383553 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8383553 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8383553 | pubmed:issn | 0925-2738 | lld:pubmed |
| pubmed-article:8383553 | pubmed:author | pubmed-author:KapteinRR | lld:pubmed |
| pubmed-article:8383553 | pubmed:author | pubmed-author:BoelensRR | lld:pubmed |
| pubmed-article:8383553 | pubmed:author | pubmed-author:van der... | lld:pubmed |
| pubmed-article:8383553 | pubmed:author | pubmed-author:KatahiraMM | lld:pubmed |
| pubmed-article:8383553 | pubmed:author | pubmed-author:SchilthuisJ... | lld:pubmed |
| pubmed-article:8383553 | pubmed:author | pubmed-author:KnegtelR MRM | lld:pubmed |
| pubmed-article:8383553 | pubmed:author | pubmed-author:EibDD | lld:pubmed |
| pubmed-article:8383553 | pubmed:author | pubmed-author:BonvinA MAM | lld:pubmed |
| pubmed-article:8383553 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8383553 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:8383553 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8383553 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8383553 | pubmed:pagination | 1-17 | lld:pubmed |
| pubmed-article:8383553 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8383553 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8383553 | pubmed:articleTitle | The solution structure of the human retinoic acid receptor-beta DNA-binding domain. | lld:pubmed |
| pubmed-article:8383553 | pubmed:affiliation | Department of Chemistry, University of Utrecht, The Netherlands. | lld:pubmed |
| pubmed-article:8383553 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8383553 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| literatureCitation:229_8383... | literatureCitation:pubmed | pubmed-article:8383553 | lld:drugbank |
| entrez-gene:5915 | entrezgene:pubmed | pubmed-article:8383553 | lld:entrezgene |
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