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1k4w

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[[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==
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The line below this paragraph, containing "STRUCTURE_1k4w", creates the "Structure Box" on the page.
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<StructureSection load='1k4w' size='340' side='right'caption='[[1k4w]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1k4w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K4W FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=STE:STEARIC+ACID'>STE</scene></td></tr>
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{{STRUCTURE_1k4w| PDB=1k4w | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4w OCA], [https://pdbe.org/1k4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k4w RCSB], [https://www.ebi.ac.uk/pdbsum/1k4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k4w ProSAT]</span></td></tr>
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</table>
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'''X-ray structure of the orphan nuclear receptor ROR beta ligand-binding domain in the active conformation'''
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== Function ==
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[https://www.uniprot.org/uniprot/RORB_RAT RORB_RAT] Orphan nuclear receptor required for normal postnatal development of rod and cone photoreceptor cells. Regulates transcription of OPN1SW in cone photoreceptor cells by binding the sequence 5'-AGGTCA-3' in the OPN1SW promoter.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k4/1k4w_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k4w ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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.
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.
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==About this Structure==
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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<ref>PMID:11689423</ref>
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1K4W is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4W OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11689423 11689423]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1k4w" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Greiner, E.]]
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[[Category: Greiner E]]
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[[Category: Moras, D.]]
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[[Category: Moras D]]
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[[Category: Renaud, J P.]]
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[[Category: Renaud JP]]
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[[Category: Schuele, R.]]
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[[Category: Schuele R]]
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[[Category: Stehlin, C.]]
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[[Category: Stehlin C]]
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[[Category: Steinmetz, A.]]
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[[Category: Steinmetz A]]
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[[Category: Wurtz, J M.]]
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[[Category: Wurtz JM]]
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[[Category: Alpha-helical sandwich]]
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[[Category: Ligand-binding domain]]
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[[Category: Transcriptionally active conformation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:18:43 2008''
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Current revision

X-ray structure of the orphan nuclear receptor ROR beta ligand-binding domain in the active conformation

PDB ID 1k4w

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