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| | <StructureSection load='1k4w' size='340' side='right'caption='[[1k4w]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1k4w' size='340' side='right'caption='[[1k4w]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1k4w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1K4W FirstGlance]. <br> | + | <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> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2lbd|2lbd]]</div></td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NR1F2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
| + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1k4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4w OCA], [http://pdbe.org/1k4w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k4w RCSB], [http://www.ebi.ac.uk/pdbsum/1k4w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k4w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Greiner, E]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Moras, D]] | + | [[Category: Greiner E]] |
| - | [[Category: Renaud, J P]] | + | [[Category: Moras D]] |
| - | [[Category: Schuele, R]] | + | [[Category: Renaud JP]] |
| - | [[Category: Stehlin, C]] | + | [[Category: Schuele R]] |
| - | [[Category: Steinmetz, A]] | + | [[Category: Stehlin C]] |
| - | [[Category: Wurtz, J M]] | + | [[Category: Steinmetz A]] |
| - | [[Category: Alpha-helical sandwich]]
| + | [[Category: Wurtz JM]] |
| - | [[Category: Hormone-growth factor complex]]
| + | |
| - | [[Category: Ligand-binding domain]]
| + | |
| - | [[Category: Transcriptionally active conformation]]
| + | |
| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stehlin C, Wurtz JM, Steinmetz A, Greiner E, Schule R, Moras D, Renaud JP. X-ray structure of the orphan nuclear receptor RORbeta ligand-binding domain in the active conformation. EMBO J. 2001 Nov 1;20(21):5822-31. PMID:11689423 doi:10.1093/emboj/20.21.5822
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