1k4w
From Proteopedia
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|PDB= 1k4w |SIZE=350|CAPTION= <scene name='initialview01'>1k4w</scene>, resolution 1.90Å | |PDB= 1k4w |SIZE=350|CAPTION= <scene name='initialview01'>1k4w</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=STE:STEARIC ACID'>STE</scene> | + | |LIGAND= <scene name='pdbligand=STE:STEARIC+ACID'>STE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= NR1F2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= NR1F2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[2lbd|2LBD]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4w OCA], [http://www.ebi.ac.uk/pdbsum/1k4w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k4w RCSB]</span> | ||
}} | }} | ||
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[[Category: Steinmetz, A.]] | [[Category: Steinmetz, A.]] | ||
[[Category: Wurtz, J M.]] | [[Category: Wurtz, J M.]] | ||
- | [[Category: STE]] | ||
[[Category: alpha-helical sandwich]] | [[Category: alpha-helical sandwich]] | ||
[[Category: ligand-binding domain]] | [[Category: ligand-binding domain]] | ||
[[Category: transcriptionally active conformation]] | [[Category: transcriptionally active conformation]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:43:26 2008'' |
Revision as of 18:43, 30 March 2008
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, resolution 1.90Å | |||||||
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Ligands: | |||||||
Gene: | NR1F2 (Rattus norvegicus) | ||||||
Related: | 2LBD
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
X-ray structure of the orphan nuclear receptor ROR beta ligand-binding domain in the active conformation
Overview
The retinoic acid-related orphan receptor beta (RORbeta) exhibits a highly restricted neuronal-specific expression pattern in brain, retina and pineal gland. So far, neither a natural RORbeta target gene nor a functional ligand have been identified, and the physiological role of the receptor is not well understood. We present the crystal structure of the ligand-binding domain (LBD) of RORbeta containing a bound stearate ligand and complexed with a coactivator peptide. In the crystal, the monomeric LBD adopts the canonical agonist-bound form. The fatty acid ligand-coactivator peptide combined action stabilizes the transcriptionally active conformation. The large ligand-binding pocket is strictly hydrophobic on the AF-2 side and more polar on the beta-sheet side where the carboxylate group of the ligand binds. Site-directed mutagenesis experiments validate the significance of the present structure. Homology modeling of the other isotypes will help to design isotype-selective agonists and antagonists that can be used to characterize the physiological functions of RORs. In addition, our crystallization strategy can be extended to other orphan nuclear receptors, providing a powerful tool to delineate their functions.
About this Structure
1K4W is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
X-ray structure of the orphan nuclear receptor RORbeta ligand-binding domain in the active conformation., Stehlin C, Wurtz JM, Steinmetz A, Greiner E, Schule R, Moras D, Renaud JP, EMBO J. 2001 Nov 1;20(21):5822-31. PMID:11689423
Page seeded by OCA on Sun Mar 30 21:43:26 2008