1yp0

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|ACTIVITY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yp0 OCA], [http://www.ebi.ac.uk/pdbsum/1yp0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yp0 RCSB]</span>
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[[Category: Suino, K.]]
[[Category: Suino, K.]]
[[Category: Xu, H.]]
[[Category: Xu, H.]]
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[[Category: PEF]]
 
[[Category: helical sandwich fold]]
[[Category: helical sandwich fold]]
[[Category: lbd fold]]
[[Category: lbd fold]]
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[[Category: steroidogenic factor-1]]
[[Category: steroidogenic factor-1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:25:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:16:09 2008''

Revision as of 22:16, 30 March 2008


PDB ID 1yp0

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of the steroidogenic factor-1 ligand binding domain bound to phospholipid and a SHP peptide motif


Overview

The orphan nuclear receptor steroidogenic factor 1 (SF-1) regulates the differentiation and function of endocrine glands. Although SF-1 is constitutively active in cell-based assays, it is not known whether this transcriptional activity is modulated by ligands. Here, we describe the 1.5 angstroms crystal structure of the SF-1 ligand binding domain in complex with an LXXLL motif from a coregulator protein. The structure reveals the presence of a phospholipid ligand in a surprisingly large pocket (approximately 1600 angstroms3), with the receptor adopting the canonical active conformation. The bound phospholipid is readily exchanged and modulates SF-1 interactions with coactivators. Mutations designed to reduce the size of the SF-1 pocket or to disrupt hydrogen bonds with the phospholipid abolish SF-1/coactivator interactions and significantly reduce SF-1 transcriptional activity. These findings provide evidence that SF-1 is regulated by endogenous ligands and suggest an unexpected relationship between phospholipids and endocrine development and function.

About this Structure

1YP0 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystallographic identification and functional characterization of phospholipids as ligands for the orphan nuclear receptor steroidogenic factor-1., Li Y, Choi M, Cavey G, Daugherty J, Suino K, Kovach A, Bingham NC, Kliewer SA, Xu HE, Mol Cell. 2005 Feb 18;17(4):491-502. PMID:15721253

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