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1k4w
From Proteopedia
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[[Image:1k4w.gif|left|200px]] | [[Image:1k4w.gif|left|200px]] | ||
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'''X-ray structure of the orphan nuclear receptor ROR beta ligand-binding domain in the active conformation''' | '''X-ray structure of the orphan nuclear receptor ROR beta ligand-binding domain in the active conformation''' | ||
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[[Category: Steinmetz, A.]] | [[Category: Steinmetz, A.]] | ||
[[Category: Wurtz, J M.]] | [[Category: Wurtz, J M.]] | ||
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| - | [[Category: | + | [[Category: Ligand-binding domain]] |
| - | [[Category: | + | [[Category: Transcriptionally active conformation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:18:43 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:18, 2 May 2008
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 Fri May 2 22:18:43 2008
