1g5y

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[[Image:1g5y.png|left|200px]]
 
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==THE 2.0 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN TETRAMER IN THE PRESENCE OF A NON-ACTIVATING RETINOIC ACID ISOMER.==
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The line below this paragraph, containing "STRUCTURE_1g5y", creates the "Structure Box" on the page.
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<StructureSection load='1g5y' size='340' side='right'caption='[[1g5y]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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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'>[[1g5y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G5Y FirstGlance]. <br>
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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]] 2&#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=REA:RETINOIC+ACID'>REA</scene></td></tr>
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{{STRUCTURE_1g5y| PDB=1g5y | 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=1g5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5y OCA], [https://pdbe.org/1g5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g5y RCSB], [https://www.ebi.ac.uk/pdbsum/1g5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g5y ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RXRA_HUMAN RXRA_HUMAN] Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes.<ref>PMID:10195690</ref> <ref>PMID:11162439</ref> <ref>PMID:11915042</ref> <ref>PMID:20215566</ref>
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== Evolutionary Conservation ==
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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/g5/1g5y_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1g5y 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 ==
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The 9-cis-retinoic acid receptors (RXRalpha, RXRbeta, and RXRgamma) are nuclear receptors that play key roles in multiple hormone-signaling pathways. Biochemical data indicate that, in the absence of ligand, RXR can exist as an inactive tetramer and that its dissociation, induced by ligand, is important for receptor activation. In this article we report the inactivated tetramer structures of the RXRalpha ligand-binding domain (LBD), either in the absence of or in the presence of a nonactivating ligand. These structures reveal that the RXR LBD tetramer forms a compact, disc-shaped complex, consisting of two symmetric dimers that are packed along helices 3 and 11. In each monomer, the AF-2 helix protrudes away from the core domain and spans into the coactivator binding site in the adjacent monomer of the symmetric dimer. In this configuration, the AF-2 helix physically excludes the binding of coactivators and suggests an autorepression mechanism that is mediated by the AF-2 helix within the tetramer. The RXR-tetramer interface is assembled from amino acids that are conserved across several closely related receptors, including the HNF4s and COUP transcription factors, and may therefore provide a model for understanding structure and regulation of this subfamily of nuclear receptors.
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===THE 2.0 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN TETRAMER IN THE PRESENCE OF A NON-ACTIVATING RETINOIC ACID ISOMER.===
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Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix.,Gampe RT Jr, Montana VG, Lambert MH, Wisely GB, Milburn MV, Xu HE Genes Dev. 2000 Sep 1;14(17):2229-41. PMID:10970886<ref>PMID:10970886</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1g5y" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10970886}}, adds the Publication Abstract to the page
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*[[Retinoid X receptor 3D structures|Retinoid X receptor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10970886 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10970886}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1G5Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G5Y OCA].
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==Reference==
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Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix., Gampe RT Jr, Montana VG, Lambert MH, Wisely GB, Milburn MV, Xu HE, Genes Dev. 2000 Sep 1;14(17):2229-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10970886 10970886]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Jr., R T.Gampe.]]
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[[Category: Gampe Jr RT]]
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[[Category: Lambert, M H.]]
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[[Category: Lambert MH]]
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[[Category: Milburn, M V.]]
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[[Category: Milburn MV]]
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[[Category: Montana, V G.]]
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[[Category: Montana VG]]
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[[Category: Wisely, G B.]]
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[[Category: Wisely GB]]
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[[Category: Xu, H E.]]
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[[Category: Xu HE]]
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[[Category: Crystal structure]]
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[[Category: Inactive tetramer with 2 monomers bound with an inactivating isomer of retinoic acid]]
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[[Category: Rxralpha ligand binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:29:55 2008''
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Current revision

THE 2.0 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN TETRAMER IN THE PRESENCE OF A NON-ACTIVATING RETINOIC ACID ISOMER.

PDB ID 1g5y

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