1YMT

Mouse SF-1 LBD

Summary for 1YMT

• Entry DOI: 10.2210/pdb1ymt/pdb
• Descriptor: Steroidogenic factor 1, Nuclear receptor 0B2, 1-CIS-9-OCTADECANOYL-2-CIS-9-HEXADECANOYL PHOSPHATIDYL GLYCEROL, ... (4 entities in total)
• Functional Keywords: nuclear receptor, sf-1, ligand-binding domain, ligand, phosphatidyl glycerol, co-repressor peptide, transcription
• Biological source: Mus musculus (house mouse); More
• Cellular location: Nucleus: P33242 Q62227
• Total number of polymer chains: 2
• Total formula weight: 30325.16

Authors

Krylova, I.N.,Sablin, E.P.,Moore, J.,Xu, R.X.,Waitt, G.M.,Juzumiene, D.,Bynum, J.M.,Fletterick, R.J.,Willson, T.M.,Ingraham, H.A. (deposition date: 2005-01-21, release date: 2005-03-15, Last modification date: 2023-08-23)

Primary citation

Krylova, I.N.,Sablin, E.P.,Moore, J.,Xu, R.X.,Waitt, G.M.,MacKay, J.A.,Juzumiene, D.,Bynum, J.M.,Madauss, K.,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

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

Experimental method

X-RAY DIFFRACTION (1.2 Å)