1yok

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Revision as of 18:15, 12 November 2007

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spinqualitylabelsall models 1yok, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

crystal structure of human LRH-1 bound with TIF-2 peptide and phosphatidylglycerol

Overview

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.

About this Structure

1YOK is a Protein complex structure of sequences from Homo sapiens with P6L as ligand. Full crystallographic information is available from OCA.

Reference

Structural analyses reveal phosphatidyl inositols as ligands for the NR5 orphan receptors SF-1 and LRH-1., Krylova IN, Sablin EP, Moore J, Xu RX, Waitt GM, MacKay JA, Juzumiene D, Bynum JM, Madauss K, Montana V, Lebedeva L, Suzawa M, Williams JD, Williams SP, Guy RK, Thornton JW, Fletterick RJ, Willson TM, Ingraham HA, Cell. 2005 Feb 11;120(3):343-55. PMID:15707893

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