| pubmed-article:7727406 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7727406 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7727406 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:7727406 | lifeskim:mentions | umls-concept:C0140279 | lld:lifeskim |
| pubmed-article:7727406 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:7727406 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7727406 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:7727406 | pubmed:dateCreated | 1995-6-1 | lld:pubmed |
| pubmed-article:7727406 | pubmed:abstractText | The ligand-dependent transactivating properties of retinoic acid receptors are controlled through a complex structure at the C-terminus of these proteins, commonly referred to as the hormone binding domain. This domain is involved not only in ligand recognition but also in protein-protein interactions such as homo- and heterodimerization processes. To identify more precisely regions of the human all-trans-retinoic acid receptor alpha (hRAR alpha) that are involved in ligand binding, we constructed a series of deletion mutants of this molecule and overexpressed them in bacteria. We found that the C-terminal part of the D domain (amino acids 186-198) was necessary for ligand binding. The F domain and the 10 C-terminal amino acids of the E domain were dispensable for high-affinity binding of various natural and synthetic retinoids. A further deletion to position 403 resulted in a moderate decrease in affinity for all-trans-(ATRA) and 9-cis-retinoic acids, whereas the binding of two RAR alpha-specific ligands (Am80 and Am580) was abolished. In addition, hRAR alpha and the minimal hormone binding domain (amino acids 186-410) bound ATRA with a positive, cooperative mechanism. This behavior was not observed with CD367, a conformationally restricted synthetic retinoid. The positive cooperativity could be correlated with stable ATRA binding to RAR homodimers, whose formation was triggered by ligand. In the same conditions, only monomeric CD367-RAR alpha complexes were detected. These data indicate that ligand binding to hRAR alpha requires the presence of part of the D domain, whereas the C-terminal end of the E domain is involved in more subtle ligand recognition processes.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:7727406 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7727406 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7727406 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7727406 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7727406 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7727406 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:7727406 | pubmed:author | pubmed-author:FormstecherPP | lld:pubmed |
| pubmed-article:7727406 | pubmed:author | pubmed-author:LefebvrePP | lld:pubmed |
| pubmed-article:7727406 | pubmed:author | pubmed-author:LefebvreBB | lld:pubmed |
| pubmed-article:7727406 | pubmed:author | pubmed-author:RachezCC | lld:pubmed |
| pubmed-article:7727406 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7727406 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:7727406 | pubmed:volume | 34 | lld:pubmed |
| pubmed-article:7727406 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7727406 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7727406 | pubmed:pagination | 5477-85 | lld:pubmed |
| pubmed-article:7727406 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:7727406 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7727406 | pubmed:articleTitle | Structural determinants of the ligand-binding site of the human retinoic acid receptor alpha. | lld:pubmed |
| pubmed-article:7727406 | pubmed:affiliation | CJF-INSERM 92-03, Laboratoire de Biochimie Structurale, Faculté de Médecine de Lille, France. | lld:pubmed |
| pubmed-article:7727406 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7727406 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7727406 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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