1g1u - Revision history

OCA at 11:19, 27 March 2024

OCA — Wed, 27 Mar 2024 11:19:00 GMT

←Older revision		Revision as of 11:19, 27 March 2024
Line 3:		Line 3:
	<StructureSection load='1g1u' size='340' side='right'caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1g1u' size='340' side='right'caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1g1u]] 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=1G1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1U FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>[[1lbd\|1lbd]]~~, [[~~1fm6~~\|~~1fm6~~]]~~, [[1fm9\|1fm9]]</div>~~</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]] 2.5Å</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=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [https://pdbe.org/1g1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [https://www.ebi.ac.uk/pdbsum/1g1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1u ProSAT]</span></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=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [https://pdbe.org/1g1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [https://www.ebi.ac.uk/pdbsum/1g1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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>	+	[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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 19:
	</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=1g1u ConSurf].		</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=1g1u ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	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.
-
-	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>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1g1u" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Gampe~~, R T~~]]	+	[[Category: Gampe Jr RT]]
-	[[Category: Lambert~~, M H~~]]	+	[[Category: Lambert MH]]
-	[[Category: Milburn~~, M V~~]]	+	[[Category: Milburn MV]]
-	[[Category: Montana~~, V G~~]]	+	[[Category: Montana VG]]
-	[[Category: Wisely~~, G B~~]]	+	[[Category: Wisely GB]]
-	[[Category: Xu~~, H E]]~~	+	[[Category: Xu HE]]
-	~~[[Category: Absence of ligand]]~~	+
-	~~[[Category: Rxralpha ligand binding domain]]~~	+
-	~~[[Category: Tetramer]]~~	+
-	~~[[Category: Transcription~~]]	+

OCA at 07:10, 24 March 2021

OCA — Wed, 24 Mar 2021 07:10:43 GMT

←Older revision		Revision as of 07:10, 24 March 2021
Line 3:		Line 3:
	<StructureSection load='1g1u' size='340' side='right'caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1g1u' size='340' side='right'caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1U OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1G1U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1U FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [~~http~~://pdbe.org/1g1u PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1g1u PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1u ProSAT]</span></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=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [https://pdbe.org/1g1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [https://www.ebi.ac.uk/pdbsum/1g1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://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>	+	[[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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[Retinoid X receptor\|Retinoid X receptor]]	+	*[[Retinoid X receptor 3D structures\|Retinoid X receptor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:35, 19 June 2019

OCA — Wed, 19 Jun 2019 07:35:56 GMT

←Older revision		Revision as of 07:35, 19 June 2019
Line 1:		Line 1:

	==THE 2.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN IN TETRAMER IN THE ABSENCE OF LIGAND==		==THE 2.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN IN TETRAMER IN THE ABSENCE OF LIGAND==
-	<StructureSection load='1g1u' size='340' side='right' caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='1g1u' size='340' side='right'caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1U FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://pdbe.org/1g1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1u ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://pdbe.org/1g1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1u ProSAT]</span></td></tr>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/1g1u_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/1g1u_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 35:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Gampe, R T]]		[[Category: Gampe, R T]]
	[[Category: Lambert, M H]]		[[Category: Lambert, M H]]

OCA at 10:58, 13 September 2017

OCA — Wed, 13 Sep 2017 10:58:02 GMT

←Older revision		Revision as of 10:58, 13 September 2017
Line 1:		Line 1:
		+
	==THE 2.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN IN TETRAMER IN THE ABSENCE OF LIGAND==		==THE 2.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN IN TETRAMER IN THE ABSENCE OF LIGAND==
	<StructureSection load='1g1u' size='340' side='right' caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1g1u' size='340' side='right' caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Human Human]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1U FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://pdbe.org/1g1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://pdbe.org/1g1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=1g1u ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Human]]
	[[Category: Gampe, R T]]		[[Category: Gampe, R T]]
	[[Category: Lambert, M H]]		[[Category: Lambert, M H]]

OCA at 08:52, 11 September 2015

OCA — Fri, 11 Sep 2015 08:52:52 GMT

←Older revision		Revision as of 08:52, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1g1u' size='340' side='right' caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1g1u' size='340' side='right' caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure with 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=1G1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1U FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://pdbe.org/1g1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1g1u" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Gampe, R T]]		[[Category: Gampe, R T]]
	[[Category: Lambert, M H]]		[[Category: Lambert, M H]]

OCA at 14:07, 25 December 2014

OCA — Thu, 25 Dec 2014 14:07:26 GMT

←Older revision		Revision as of 14:07, 25 December 2014
Line 6:		Line 6:
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 23:18, 22 December 2014

OCA — Mon, 22 Dec 2014 23:18:12 GMT

←Older revision		Revision as of 23:18, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure with 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=1G1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1U FirstGlance]. <br>		<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure with 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=1G1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1U FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Gampe, R T.]]	+	[[Category: Gampe, R T]]
-	[[Category: Lambert, M H.]]	+	[[Category: Lambert, M H]]
-	[[Category: Milburn, M V.]]	+	[[Category: Milburn, M V]]
-	[[Category: Montana, V G.]]	+	[[Category: Montana, V G]]
-	[[Category: Wisely, G B.]]	+	[[Category: Wisely, G B]]
-	[[Category: Xu, H E.]]	+	[[Category: Xu, H E]]
	[[Category: Absence of ligand]]		[[Category: Absence of ligand]]
	[[Category: Rxralpha ligand binding domain]]		[[Category: Rxralpha ligand binding domain]]
	[[Category: Tetramer]]		[[Category: Tetramer]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 12:59, 28 September 2014

OCA — Sun, 28 Sep 2014 12:59:43 GMT

←Older revision		Revision as of 12:59, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1g1u.~~png~~\|~~left~~\|200px]]	+	==THE 2.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN IN TETRAMER IN THE ABSENCE OF LIGAND==
		+	<StructureSection load='1g1u' size='340' side='right' caption='[[1g1u]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1g1u]] is a 4 chain structure with 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=1G1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1U FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lbd\|1lbd]], [[1fm6\|1fm6]], [[1fm9\|1fm9]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g1u RCSB], [http://www.ebi.ac.uk/pdbsum/1g1u PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/1g1u_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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.

-	~~{{STRUCTURE_1g1u\| PDB=1g1u \| SCENE= }}~~	+	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>

-	~~===THE 2.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN IN TETRAMER IN THE ABSENCE OF LIGAND===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_10970886}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1g1u]] is~~ a ~~4 chain structure with 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=1G1U OCA].~~	+

	==See Also==		==See Also==
	*[[Retinoid X receptor\|Retinoid X receptor]]		*[[Retinoid X receptor\|Retinoid X receptor]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:010970886<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Gampe, R T.]]		[[Category: Gampe, R T.]]

OCA: Protected "1g1u" [edit=sysop:move=sysop]

OCA — Sat, 20 Oct 2012 17:37:17 GMT

Protected "1g1u" [edit=sysop:move=sysop]

←Older revision

Revision as of 17:37, 20 October 2012

OCA at 17:37, 20 October 2012

OCA — Sat, 20 Oct 2012 17:37:16 GMT

←Older revision		Revision as of 17:37, 20 October 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1g1u.png\|left\|200px]]		[[Image:1g1u.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1g1u", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1g1u\| PDB=1g1u \| SCENE= }}		{{STRUCTURE_1g1u\| PDB=1g1u \| SCENE= }}

	===THE 2.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN IN TETRAMER IN THE ABSENCE OF LIGAND===		===THE 2.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN IN TETRAMER IN THE ABSENCE OF LIGAND===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_10970886}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 10970886 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_10970886}}		{{ABSTRACT_PUBMED_10970886}}

	==About this Structure==		==About this Structure==
-	~~1G1U~~ is a 4 ~~chains~~ structure ~~of sequences~~ 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=1G1U OCA].	+	[[1g1u]] is a 4 chain structure with 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=1G1U OCA].
		+
		+	==See Also==
		+	*[[Retinoid X receptor\|Retinoid X receptor]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~10970886~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010970886</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: ~~Jr.~~, R T~~.Gampe~~.]]	+	[[Category: Gampe, R T.]]
	[[Category: Lambert, M H.]]		[[Category: Lambert, M H.]]
	[[Category: Milburn, M V.]]		[[Category: Milburn, M V.]]
Line 32:		Line 23:
	[[Category: Xu, H E.]]		[[Category: Xu, H E.]]
	[[Category: Absence of ligand]]		[[Category: Absence of ligand]]
-	[[Category: Crystal structure]]
	[[Category: Rxralpha ligand binding domain]]		[[Category: Rxralpha ligand binding domain]]
	[[Category: Tetramer]]		[[Category: Tetramer]]
-		+	[[Category: Transcription]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 18:15:14 2009''~~	+