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1YOW

human Steroidogenic Factor 1 LBD with bound Co-factor Peptide

Summary for 1YOW
Entry DOI10.2210/pdb1yow/pdb
DescriptorSteroidogenic factor 1, TIF2 peptide, PHOSPHATIDYL ETHANOL, ... (4 entities in total)
Functional Keywordssteroidogenic factor 1, sf1, phospholipid, phosphatidyl ethanolamine, phosphatidyl glycerol, transcription
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus : Q13285
Total number of polymer chains2
Total formula weight29500.58
Authors
Primary citationKrylova, I.N.,Sablin, E.P.,Xu, R.X.,Waitt, G.M.,MacKay, J.A.,Juzumiene, D.,Bynum, J.M.,Madauss, K.P.,Montana, V.,Lebedeva, L.,Suzawa, M.,Williams, J.D.,Williams, S.P.,Guy, R.K.,Thornton, J.W.,Fletterick, R.J.,Willson, T.M.,Ingraham, H.A.
Structural analyses reveal phosphatidyl inositols as ligands for the NR5 orphan receptors SF-1 and LRH-1
Cell(Cambridge,Mass.), 120:343-355, 2005
Cited by
PubMed Abstract: Vertebrate members of the nuclear receptor NR5A subfamily, which includes steroidogenic factor 1 (SF-1) and liver receptor homolog 1 (LRH-1), regulate crucial aspects of development, endocrine homeostasis, and metabolism. Mouse LRH-1 is believed to be a ligand-independent transcription factor with a large and empty hydrophobic pocket. Here we present structural and biochemical data for three other NR5A members-mouse and human SF-1 and human LRH-1-which reveal that these receptors bind phosphatidyl inositol second messengers and that ligand binding is required for maximal activity. Evolutionary analysis of structure-function relationships across the SF-1/LRH-1 subfamily indicates that ligand binding is the ancestral state of NR5A receptors and was uniquely diminished or altered in the rodent LRH-1 lineage. We propose that phospholipids regulate gene expression by directly binding to NR5A nuclear receptors.
PubMed: 15707893
DOI: 10.1016/j.cell.2005.01.024
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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