1ymt

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(New page: 200px<br /><applet load="1ymt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ymt, resolution 1.20&Aring;" /> '''Mouse SF-1 LBD'''<br...)
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[[Image:1ymt.gif|left|200px]]<br /><applet load="1ymt" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ymt.gif|left|200px]]<br /><applet load="1ymt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ymt, resolution 1.20&Aring;" />
caption="1ymt, resolution 1.20&Aring;" />
'''Mouse SF-1 LBD'''<br />
'''Mouse SF-1 LBD'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1YMT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with DR9 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YMT OCA].
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1YMT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=DR9:'>DR9</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMT OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Bynum, J.M.]]
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[[Category: Bynum, J M.]]
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[[Category: Fletterick, R.J.]]
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[[Category: Fletterick, R J.]]
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[[Category: Ingraham, H.A.]]
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[[Category: Ingraham, H A.]]
[[Category: Juzumiene, D.]]
[[Category: Juzumiene, D.]]
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[[Category: Krylova, I.N.]]
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[[Category: Krylova, I N.]]
[[Category: Moore, J.]]
[[Category: Moore, J.]]
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[[Category: Sablin, E.P.]]
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[[Category: Sablin, E P.]]
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[[Category: Waitt, G.M.]]
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[[Category: Waitt, G M.]]
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[[Category: Willson, T.M.]]
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[[Category: Willson, T M.]]
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[[Category: Xu, R.X.]]
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[[Category: Xu, R X.]]
[[Category: DR9]]
[[Category: DR9]]
[[Category: co-repressor peptide]]
[[Category: co-repressor peptide]]
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[[Category: sf-1]]
[[Category: sf-1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:55:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:55 2008''

Revision as of 14:06, 21 February 2008


1ymt, resolution 1.20Å

Drag the structure with the mouse to rotate

Mouse SF-1 LBD

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

1YMT is a Protein complex structure of sequences from Mus musculus with 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

Page seeded by OCA on Thu Feb 21 16:06:55 2008

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