| pubmed-article:15897460 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15897460 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:15897460 | lifeskim:mentions | umls-concept:C0023884 | lld:lifeskim |
| pubmed-article:15897460 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:15897460 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:15897460 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:15897460 | pubmed:dateCreated | 2005-5-25 | lld:pubmed |
| pubmed-article:15897460 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15897460 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15897460 | pubmed:abstractText | Steroidogenic factor-1 (SF-1) and liver receptor homologue-1 (LRH-1) belong to the fushi tarazu factor 1 subfamily of nuclear receptors. SF-1 is an essential factor for sex determination during development and regulates adrenal and gonadal steroidogenesis in the adult, whereas LRH-1 is a critical factor for development of endodermal tissues and regulates cholesterol and bile acid homeostasis. Regulatory ligands are unknown for SF-1 and LRH-1. A reported mouse LRH-1 structure revealed an empty pocket in a region commonly occupied by ligands in the structures of other nuclear receptors, and pocket-filling mutations did not alter the constitutive activity observed. Here we report the crystal structures of the putative ligand-binding domains of human SF-1 at 2.1-A resolution and human LRH-1 at 2.5-A resolution. Both structures bind a coactivator-derived peptide at the canonical activation-function surface, thus adopting the transcriptionally activating conformation. In human LRH-1, coactivator peptide binding also occurs to a second site. We discovered in both structures a phospholipid molecule bound in a pocket of the putative ligand-binding domain. MS analysis of the protein samples used for crystallization indicated that the two proteins associate with a range of phospholipids. Mutations of the pocket-lining residues reduced the transcriptional activities of SF-1 and LRH-1 in mammalian cell transfection assays without affecting their expression levels. These results suggest that human SF-1 and LRH-1 may be ligand-binding receptors, although it remains to be seen if phospholipids or possibly other molecules regulate SF-1 or LRH-1 under physiological conditions. | lld:pubmed |
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| pubmed-article:15897460 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15897460 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15897460 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15897460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15897460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15897460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15897460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15897460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15897460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15897460 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15897460 | pubmed:month | May | lld:pubmed |
| pubmed-article:15897460 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:ZhangChaoC | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:WestBrian LBL | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:MarimuthuAdhi... | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:NguyenHoaH | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:KrupkaHeike... | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:EngKevinK | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:WangWeiruW | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:MehraUpasanaU | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:MilburnMichae... | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:PowellBenB | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:TabrizizadMar... | lld:pubmed |
| pubmed-article:15897460 | pubmed:author | pubmed-author:ShelloeRafeR | lld:pubmed |
