4tuz - Revision history

OCA at 12:24, 20 December 2023

OCA — Wed, 20 Dec 2023 12:24:51 GMT

←Older revision		Revision as of 12:24, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4tuz]] 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=4TUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TUZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4tuz]] 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=4TUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TUZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=36J:(3S,7R,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE'>36J</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=36J:(3S,7R,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE'>36J</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=4tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tuz OCA], [https://pdbe.org/4tuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tuz RCSB], [https://www.ebi.ac.uk/pdbsum/4tuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tuz 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=4tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tuz OCA], [https://pdbe.org/4tuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tuz RCSB], [https://www.ebi.ac.uk/pdbsum/4tuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tuz ProSAT]</span></td></tr>
	</table>		</table>

OCA at 10:56, 15 March 2023

OCA — Wed, 15 Mar 2023 10:56:46 GMT

←Older revision		Revision as of 10:56, 15 March 2023
Line 3:		Line 3:
	<StructureSection load='4tuz' size='340' side='right'caption='[[4tuz]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4tuz' size='340' side='right'caption='[[4tuz]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4tuz]] 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=4TUZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4TUZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4tuz]] 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=4TUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TUZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=36J:(3S,7R,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE'>36J</scene>, <scene name='pdbligand=~~EDO~~:~~1,2~~-~~ETHANEDIOL~~'>~~EDO~~</scene>, <scene name='pdbligand=~~GOL~~:~~GLYCEROL~~'>~~GOL~~</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=36J:(3S,7R,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE'>36J</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=~~CSO~~:~~S-HYDROXYCYSTEINE~~'>~~CSO~~</scene~~></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=4tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tuz OCA], [https://pdbe.org/4tuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tuz RCSB], [https://www.ebi.ac.uk/pdbsum/4tuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tuz ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mg8\|4mg8]]</td></tr>~~	+
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ESR1, ESR, NR3A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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=4tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tuz OCA], [~~http~~://pdbe.org/4tuz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4tuz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4tuz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4tuz ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ESR1_HUMAN ESR1_HUMAN]] Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full length receptor. Isoform 3 can bind to ERE and inhibit isoform 1.<ref>PMID:7651415</ref> <ref>PMID:10970861</ref> <ref>PMID:9328340</ref> <ref>PMID:10681512</ref> <ref>PMID:10816575</ref> <ref>PMID:11477071</ref> <ref>PMID:11682626</ref> <ref>PMID:15078875</ref> <ref>PMID:16043358</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> <ref>PMID:18247370</ref> <ref>PMID:17932106</ref> <ref>PMID:19350539</ref> <ref>PMID:20705611</ref> <ref>PMID:21937726</ref> <ref>PMID:21330404</ref> <ref>PMID:22083956</ref>	+	[https://www.uniprot.org/uniprot/ESR1_HUMAN ESR1_HUMAN] Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full length receptor. Isoform 3 can bind to ERE and inhibit isoform 1.<ref>PMID:7651415</ref> <ref>PMID:10970861</ref> <ref>PMID:9328340</ref> <ref>PMID:10681512</ref> <ref>PMID:10816575</ref> <ref>PMID:11477071</ref> <ref>PMID:11682626</ref> <ref>PMID:15078875</ref> <ref>PMID:16043358</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> <ref>PMID:18247370</ref> <ref>PMID:17932106</ref> <ref>PMID:19350539</ref> <ref>PMID:20705611</ref> <ref>PMID:21937726</ref> <ref>PMID:21330404</ref> <ref>PMID:22083956</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 29:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone acetyltransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bourguet, W]]	+	[[Category: Bourguet W]]
-	[[Category: Delfosse, V]]	+	[[Category: Delfosse V]]
-	[[Category: Grimaldi, M]]	+	[[Category: Grimaldi M]]
-	~~[[Category: Nuclear hormone receptor ligand binding domain endocrine disruptor environmental compound]]~~	+
-	~~[[Category: Nuclear protein~~]]	+

OCA at 07:01, 19 February 2020

OCA — Wed, 19 Feb 2020 07:01:02 GMT

←Older revision		Revision as of 07:01, 19 February 2020
Line 1:		Line 1:

	==Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol==		==Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol==
-	<StructureSection load='4tuz' size='340' side='right' caption='[[4tuz]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='4tuz' size='340' side='right'caption='[[4tuz]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4tuz]] 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=4TUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TUZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4tuz]] 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=4TUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TUZ FirstGlance]. <br>
Line 24:		Line 24:

	==See Also==		==See Also==
-	*[[Estrogen receptor\|Estrogen receptor]]	+	*[[Estrogen receptor 3D structures\|Estrogen receptor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 31:		Line 31:
	[[Category: Histone acetyltransferase]]		[[Category: Histone acetyltransferase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bourguet, W]]		[[Category: Bourguet, W]]
	[[Category: Delfosse, V]]		[[Category: Delfosse, V]]

OCA at 15:45, 27 February 2019

OCA — Wed, 27 Feb 2019 15:45:50 GMT

←Older revision		Revision as of 15:45, 27 February 2019
Line 1:		Line 1:
		+
	==Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol==		==Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol==
	<StructureSection load='4tuz' size='340' side='right' caption='[[4tuz]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4tuz' size='340' side='right' caption='[[4tuz]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4tuz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TUZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4tuz]] 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=4TUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TUZ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=36J:(3S,7R,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE'>36J</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=36J:(3S,7R,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE'>36J</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mg8\|4mg8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mg8\|4mg8]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ESR1, ESR, NR3A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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=4tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tuz OCA], [http://pdbe.org/4tuz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tuz RCSB], [http://www.ebi.ac.uk/pdbsum/4tuz 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=4tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tuz OCA], [http://pdbe.org/4tuz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tuz RCSB], [http://www.ebi.ac.uk/pdbsum/4tuz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tuz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Histone acetyltransferase]]		[[Category: Histone acetyltransferase]]
		+	[[Category: Human]]
	[[Category: Bourguet, W]]		[[Category: Bourguet, W]]
	[[Category: Delfosse, V]]		[[Category: Delfosse, V]]

OCA at 18:50, 30 November 2015

OCA — Mon, 30 Nov 2015 18:50:52 GMT

←Older revision		Revision as of 18:50, 30 November 2015
Line 7:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mg8\|4mg8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mg8\|4mg8]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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=4tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tuz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tuz RCSB], [http://www.ebi.ac.uk/pdbsum/4tuz 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=4tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tuz OCA], [http://pdbe.org/4tuz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tuz RCSB], [http://www.ebi.ac.uk/pdbsum/4tuz PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 19:
	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 4tuz" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Estrogen receptor\|Estrogen receptor]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:37, 28 January 2015

OCA — Wed, 28 Jan 2015 16:37:12 GMT

←Older revision		Revision as of 16:37, 28 January 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol==
		+	<StructureSection load='4tuz' size='340' side='right' caption='[[4tuz]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4tuz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TUZ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=36J:(3S,7R,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE'>36J</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mg8\|4mg8]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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=4tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tuz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tuz RCSB], [http://www.ebi.ac.uk/pdbsum/4tuz PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ESR1_HUMAN ESR1_HUMAN]] Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full length receptor. Isoform 3 can bind to ERE and inhibit isoform 1.<ref>PMID:7651415</ref> <ref>PMID:10970861</ref> <ref>PMID:9328340</ref> <ref>PMID:10681512</ref> <ref>PMID:10816575</ref> <ref>PMID:11477071</ref> <ref>PMID:11682626</ref> <ref>PMID:15078875</ref> <ref>PMID:16043358</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> <ref>PMID:18247370</ref> <ref>PMID:17932106</ref> <ref>PMID:19350539</ref> <ref>PMID:20705611</ref> <ref>PMID:21937726</ref> <ref>PMID:21330404</ref> <ref>PMID:22083956</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Nuclear receptors (NRs) are members of a large superfamily of evolutionarily related transcription factors that control a plethora of biological processes. NRs orchestrate complex events such as development, organ homeostasis, metabolism, immune function, and reproduction. Approximately one-half of the 48 human NRs have been shown to act as ligand-regulated transcription factors and respond directly to a large variety of endogenous hormones and metabolites that are generally hydrophobic and small in size (eg, retinoic acid or estradiol). The second half of the NR family comprises the so-called orphan receptors, for which regulatory ligands are still unknown or may not exist despite the presence of a C-terminal ligand-binding domain, which is the hallmark of all NRs. Several chemicals released into the environment (eg, bisphenols, phthalates, parabens, etc) share some physicochemical properties with natural ligands, allowing them to bind to NRs and activate or inhibit their action. Collectively referred to as endocrine disruptors or endocrine-disrupting chemicals (EDCs), these environmental pollutants are highly suspected to cause a wide range of developmental, reproductive, neurological, or metabolic defects in humans and wildlife. Crystallographic studies are revealing unanticipated mechanisms by which chemically diverse EDCs interact with the ligand-binding domain of NRs. These studies thereby provide a rational basis for designing novel chemicals with lower impacts on human and animal health. In this review, we provide a structural and mechanistic view of endocrine disrupting action using estrogen receptors alpha and beta, (ERalpha/beta), peroxisome proliferator activated receptor gamma (PPARgamma), and their respective environmental ligands as representative examples.

-	~~The entry 4tuz is ON HOLD until Paper Publication~~	+	A structural perspective on nuclear receptors as targets of environmental compounds.,Delfosse V, Maire AL, Balaguer P, Bourguet W Acta Pharmacol Sin. 2014 Dec 15. doi: 10.1038/aps.2014.133. PMID:25500867<ref>PMID:25500867</ref>

-	~~Authors: Delfosse~~, V.~~, Grimaldi, M~~.~~, Bourguet, W~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Histone acetyltransferase]]
		+	[[Category: Bourguet, W]]
	[[Category: Delfosse, V]]		[[Category: Delfosse, V]]
-	[[Category: Bourguet, W]]
	[[Category: Grimaldi, M]]		[[Category: Grimaldi, M]]
		+	[[Category: Nuclear hormone receptor ligand binding domain endocrine disruptor environmental compound]]
		+	[[Category: Nuclear protein]]

OCA at 17:53, 24 December 2014

OCA — Wed, 24 Dec 2014 17:53:18 GMT

←Older revision		Revision as of 17:53, 24 December 2014
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	Description: Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol		Description: Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol
		+	[[Category: Unreleased Structures]]
		+	[[Category: Delfosse, V]]
		+	[[Category: Bourguet, W]]
		+	[[Category: Grimaldi, M]]

OCA at 06:58, 9 July 2014

OCA — Wed, 09 Jul 2014 06:58:05 GMT

←Older revision		Revision as of 06:58, 9 July 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4tuz is ON HOLD	+	The entry 4tuz is ON HOLD until Paper Publication

	Authors: Delfosse, V., Grimaldi, M., Bourguet, W.		Authors: Delfosse, V., Grimaldi, M., Bourguet, W.

	Description: Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol		Description: Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol

OCA: Protected "4tuz" [edit=sysop:move=sysop]

OCA — Wed, 02 Jul 2014 07:35:26 GMT

Protected "4tuz" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:35, 2 July 2014

OCA: New page: '''Unreleased structure''' The entry 4tuz is ON HOLD Authors: Delfosse, V., Grimaldi, M., Bourguet, W. Description: Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalen...

OCA — Wed, 02 Jul 2014 07:35:25 GMT

New page: '''Unreleased structure''' The entry 4tuz is ON HOLD Authors: Delfosse, V., Grimaldi, M., Bourguet, W. Description: Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalen...

New page

'''Unreleased structure'''

The entry 4tuz is ON HOLD

Authors: Delfosse, V., Grimaldi, M., Bourguet, W.

Description: Crystal structure of hERa-LBD (Y537S) in complex with alpha-zearalenol