1zdu

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|PDB= 1zdu |SIZE=350|CAPTION= <scene name='initialview01'>1zdu</scene>, resolution 2.50&Aring;
|PDB= 1zdu |SIZE=350|CAPTION= <scene name='initialview01'>1zdu</scene>, resolution 2.50&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=P3A:PHOSPHATIDYLGLYCEROL-PHOSPHOGLYCEROL'>P3A</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|LIGAND= <scene name='pdbligand=P3A:PHOSPHATIDYLGLYCEROL-PHOSPHOGLYCEROL'>P3A</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1zdt|1ZDT]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zdu OCA], [http://www.ebi.ac.uk/pdbsum/1zdu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zdu RCSB]</span>
}}
}}
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[[Category: West, B L.]]
[[Category: West, B L.]]
[[Category: Zhang, C.]]
[[Category: Zhang, C.]]
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[[Category: P3A]]
 
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[[Category: TRS]]
 
[[Category: liver receptor homologue-1]]
[[Category: liver receptor homologue-1]]
[[Category: lrh-1]]
[[Category: lrh-1]]
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[[Category: phospholipid]]
[[Category: phospholipid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:34:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:34:35 2008''

Revision as of 22:34, 30 March 2008


PDB ID 1zdu

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands: ,
Related: 1ZDT


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



The Crystal Structure of Human Liver Receptor Homologue-1


Overview

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.

About this Structure

1ZDU is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structures of human steroidogenic factor-1 and liver receptor homologue-1., Wang W, Zhang C, Marimuthu A, Krupka HI, Tabrizizad M, Shelloe R, Mehra U, Eng K, Nguyen H, Settachatgul C, Powell B, Milburn MV, West BL, Proc Natl Acad Sci U S A. 2005 May 24;102(21):7505-10. Epub 2005 May 16. PMID:15897460

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