5tn9 - Revision history

OCA at 14:22, 6 March 2024

OCA — Wed, 06 Mar 2024 14:22:26 GMT

←Older revision		Revision as of 14:22, 6 March 2024
Line 1:		Line 1:

	==Crystal Structure of the ER-alpha Ligand-binding Domain (L372S,L536S) in Complex with the OBHS-BSC, 4-bromophenyl (1R,2R,4S)-5-(4-hydroxyphenyl)-6-(4-(2-(piperidin-1-yl)ethoxy)phenyl)-7-oxabicyclo[2.2.1]hept-5-ene-2-sulfonate==		==Crystal Structure of the ER-alpha Ligand-binding Domain (L372S,L536S) in Complex with the OBHS-BSC, 4-bromophenyl (1R,2R,4S)-5-(4-hydroxyphenyl)-6-(4-(2-(piperidin-1-yl)ethoxy)phenyl)-7-oxabicyclo[2.2.1]hept-5-ene-2-sulfonate==
-	<StructureSection load='5tn9' size='340' side='right' caption='[[5tn9]], [[Resolution\|resolution]] 2.25Å' scene=''>	+	<StructureSection load='5tn9' size='340' side='right'caption='[[5tn9]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tn9]] 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=5TN9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5TN9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tn9]] 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=5TN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TN9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7EC:4-BROMOPHENYL+(1S,2R,4S)-5-(4-HYDROXYPHENYL)-6-{4-[2-(PIPERIDIN-1-YL)ETHOXY]PHENYL}-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2-SULFONATE'>7EC</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]] 2.253Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5tnb\|5tnb]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7EC:4-BROMOPHENYL+(1S,2R,4S)-5-(4-HYDROXYPHENYL)-6-{4-[2-(PIPERIDIN-1-YL)ETHOXY]PHENYL}-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2-SULFONATE'>7EC</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5tn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tn9 OCA], [https://pdbe.org/5tn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tn9 RCSB], [https://www.ebi.ac.uk/pdbsum/5tn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tn9 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=5tn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tn9 OCA], [~~http~~://pdbe.org/5tn9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5tn9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5tn9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5tn9 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;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The estrogen receptors (ERs) bind with high affinity to many structurally diverse ligands by significantly distorting the contours of their ligand-binding pockets. This raises a question: To what degree is ER able to distinguish between structurally related regioisomers and enantiomers? We have explored the structural compliance and specificity of ERalpha with a set of ligands having a 7-oxa-bicyclo[2.2.1]hept-5-ene sulfonate core and basic side chains typical of selective ER modulators (SERMs). These ligands have two regioisomers, each of which is a racemate of enantiomers. Using orthogonal protecting groups and chiral HPLC, we isolated all 4 isomers and assigned their absolute stereochemistry by X-ray analysis. The 1S,2R,4S isomer has a 80-170-fold higher affinity for ERalpha than the others, and it profiles as a partial agonist/antagonist in cellular reporter gene assays and in suppressing proliferation of MCF-7 breast cancer cells with subnanomolar potency, far exceeding that of the other isomers. It is the only isomer found bound to ERalpha by X-ray analysis after crystallization with four-isomer mixtures of closely related analogs. Thus, despite the general compliance of this receptor for binding a large variety of ligand structures, ER demonstrates marked structural specificity and stereospecificity by selecting a single component from a mixture of structurally related isomers to drive ER-regulated cellular activity. Our findings lay the necessary groundwork for seeking unique ER-mediated pharmacological profiles by rational structural perturbations of two different types of side chains in this unprecedented class of ER ligands, which may prove useful in developing more effective endocrine therapies for breast cancer.	+

-	Exploring the Structural Compliancy versus Specificity of the Estrogen Receptor Using Isomeric Three-Dimensional Ligands.,Sharma N, Carlson KE, Nwachukwu JC, Srinivasan S, Sharma A, Nettles KW, Katzenellenbogen JA ACS Chem Biol. 2017 Feb 17;12(2):494-503. doi: 10.1021/acschembio.6b00918. Epub, 2016 Dec 29. PMID:28032978<ref>PMID:28032978</ref>	+	==See Also==
-		+	*[[Estrogen receptor 3D structures\|Estrogen receptor 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 5tn9" style~~=~~"background-color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Carlson~~, K E~~]]	+	[[Category: Large Structures]]
-	[[Category: Katzenellenbogen~~, J A~~]]	+	[[Category: Carlson KE]]
-	[[Category: Nettles~~, K W~~]]	+	[[Category: Katzenellenbogen JA]]
-	[[Category: Nwachukwu~~, J C~~]]	+	[[Category: Nettles KW]]
-	[[Category: Sharma, A]]	+	[[Category: Nwachukwu JC]]
-	[[Category: Sharma, N]]	+	[[Category: Sharma A]]
-	[[Category: Srinivasan, S]]	+	[[Category: Sharma N]]
-	~~[[Category: Ligand binding]]~~	+	[[Category: Srinivasan S]]
-	~~[[Category: Nuclear receptor]]~~	+
-	~~[[Category: Protein-ligand complex]]~~	+
-	~~[[Category: Transcription]]~~	+
-	~~[[Category: Transcription factor~~]]	+

OCA at 10:17, 22 November 2017

OCA — Wed, 22 Nov 2017 10:17:18 GMT

←Older revision		Revision as of 10:17, 22 November 2017
Line 3:		Line 3:
	<StructureSection load='5tn9' size='340' side='right' caption='[[5tn9]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='5tn9' size='340' side='right' caption='[[5tn9]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tn9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TN9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TN9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tn9]] 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=5TN9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TN9 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7EC:4-BROMOPHENYL+(1S,2R,4S)-5-(4-HYDROXYPHENYL)-6-{4-[2-(PIPERIDIN-1-YL)ETHOXY]PHENYL}-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2-SULFONATE'>7EC</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7EC:4-BROMOPHENYL+(1S,2R,4S)-5-(4-HYDROXYPHENYL)-6-{4-[2-(PIPERIDIN-1-YL)ETHOXY]PHENYL}-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2-SULFONATE'>7EC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5tnb\|5tnb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5tnb\|5tnb]]</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='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=5tn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tn9 OCA], [http://pdbe.org/5tn9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tn9 RCSB], [http://www.ebi.ac.uk/pdbsum/5tn9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tn9 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=5tn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tn9 OCA], [http://pdbe.org/5tn9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tn9 RCSB], [http://www.ebi.ac.uk/pdbsum/5tn9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tn9 ProSAT]</span></td></tr>
	</table>		</table>
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Carlson, K E]]		[[Category: Carlson, K E]]
	[[Category: Katzenellenbogen, J A]]		[[Category: Katzenellenbogen, J A]]

OCA at 08:07, 9 March 2017

OCA — Thu, 09 Mar 2017 08:07:33 GMT

←Older revision		Revision as of 08:07, 9 March 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5tn9 is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal Structure of the ER-alpha Ligand-binding Domain (L372S,L536S) in Complex with the OBHS-BSC, 4-bromophenyl (1R,2R,4S)-5-(4-hydroxyphenyl)-6-(4-(2-(piperidin-1-yl)ethoxy)phenyl)-7-oxabicyclo[2.2.1]hept-5-ene-2-sulfonate==
		+	<StructureSection load='5tn9' size='340' side='right' caption='[[5tn9]], [[Resolution\|resolution]] 2.25Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5tn9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TN9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TN9 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7EC:4-BROMOPHENYL+(1S,2R,4S)-5-(4-HYDROXYPHENYL)-6-{4-[2-(PIPERIDIN-1-YL)ETHOXY]PHENYL}-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2-SULFONATE'>7EC</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5tnb\|5tnb]]</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=5tn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tn9 OCA], [http://pdbe.org/5tn9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tn9 RCSB], [http://www.ebi.ac.uk/pdbsum/5tn9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tn9 ProSAT]</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 ==
		+	The estrogen receptors (ERs) bind with high affinity to many structurally diverse ligands by significantly distorting the contours of their ligand-binding pockets. This raises a question: To what degree is ER able to distinguish between structurally related regioisomers and enantiomers? We have explored the structural compliance and specificity of ERalpha with a set of ligands having a 7-oxa-bicyclo[2.2.1]hept-5-ene sulfonate core and basic side chains typical of selective ER modulators (SERMs). These ligands have two regioisomers, each of which is a racemate of enantiomers. Using orthogonal protecting groups and chiral HPLC, we isolated all 4 isomers and assigned their absolute stereochemistry by X-ray analysis. The 1S,2R,4S isomer has a 80-170-fold higher affinity for ERalpha than the others, and it profiles as a partial agonist/antagonist in cellular reporter gene assays and in suppressing proliferation of MCF-7 breast cancer cells with subnanomolar potency, far exceeding that of the other isomers. It is the only isomer found bound to ERalpha by X-ray analysis after crystallization with four-isomer mixtures of closely related analogs. Thus, despite the general compliance of this receptor for binding a large variety of ligand structures, ER demonstrates marked structural specificity and stereospecificity by selecting a single component from a mixture of structurally related isomers to drive ER-regulated cellular activity. Our findings lay the necessary groundwork for seeking unique ER-mediated pharmacological profiles by rational structural perturbations of two different types of side chains in this unprecedented class of ER ligands, which may prove useful in developing more effective endocrine therapies for breast cancer.

-	~~Authors~~:	+	Exploring the Structural Compliancy versus Specificity of the Estrogen Receptor Using Isomeric Three-Dimensional Ligands.,Sharma N, Carlson KE, Nwachukwu JC, Srinivasan S, Sharma A, Nettles KW, Katzenellenbogen JA ACS Chem Biol. 2017 Feb 17;12(2):494-503. doi: 10.1021/acschembio.6b00918. Epub, 2016 Dec 29. PMID:28032978<ref>PMID:28032978</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5tn9" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Carlson, K E]]
		+	[[Category: Katzenellenbogen, J A]]
		+	[[Category: Nettles, K W]]
		+	[[Category: Nwachukwu, J C]]
		+	[[Category: Sharma, A]]
		+	[[Category: Sharma, N]]
		+	[[Category: Srinivasan, S]]
		+	[[Category: Ligand binding]]
		+	[[Category: Nuclear receptor]]
		+	[[Category: Protein-ligand complex]]
		+	[[Category: Transcription]]
		+	[[Category: Transcription factor]]

OCA at 17:39, 9 December 2016

OCA — Fri, 09 Dec 2016 17:39:54 GMT

←Older revision		Revision as of 17:39, 9 December 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5tn9 is ON HOLD	+	The entry 5tn9 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA at 17:15, 26 October 2016

OCA — Wed, 26 Oct 2016 17:15:28 GMT

←Older revision		Revision as of 17:15, 26 October 2016
Line 3:		Line 3:
	The entry 5tn9 is ON HOLD		The entry 5tn9 is ON HOLD

-	Authors: ~~Nwachukwu, J.C., Sharma, N., Carlson, K.E., Srinivasan, S., Sharma, A., Katzenellenbogen, J.A., Nettles, K.W.~~	+	Authors:

-	Description: Crystal Structure of the ER-alpha Ligand-binding Domain (L372S,L536S) in Complex with the OBHS-BSC, 4-bromophenyl (1R,2R,4S)-5-(4-hydroxyphenyl)-6-(4-(2-(piperidin-1-yl)ethoxy)phenyl)-7-oxabicyclo[2.2.1]hept-5-ene-2-sulfonate	+	Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Sharma, N]]
-	[[Category: Nwachukwu, J.C]]
-	[[Category: Katzenellenbogen, J.A]]
-	[[Category: Srinivasan, S]]
-	[[Category: Carlson, K.E]]
-	[[Category: Sharma, A]]
-	[[Category: Nettles, K.W]]

OCA: Protected "5tn9" [edit=sysop:move=sysop]

OCA — Wed, 19 Oct 2016 16:04:49 GMT

Protected "5tn9" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:04, 19 October 2016

OCA: New page: '''Unreleased structure''' The entry 5tn9 is ON HOLD Authors: Nwachukwu, J.C., Sharma, N., Carlson, K.E., Srinivasan, S., Sharma, A., Katzenellenbogen, J.A., Nettles, K.W. Description:...

OCA — Wed, 19 Oct 2016 16:04:48 GMT

New page: '''Unreleased structure''' The entry 5tn9 is ON HOLD Authors: Nwachukwu, J.C., Sharma, N., Carlson, K.E., Srinivasan, S., Sharma, A., Katzenellenbogen, J.A., Nettles, K.W. Description:...

New page

'''Unreleased structure'''

The entry 5tn9 is ON HOLD

Authors: Nwachukwu, J.C., Sharma, N., Carlson, K.E., Srinivasan, S., Sharma, A., Katzenellenbogen, J.A., Nettles, K.W.

Description: Crystal Structure of the ER-alpha Ligand-binding Domain (L372S,L536S) in Complex with the OBHS-BSC, 4-bromophenyl (1R,2R,4S)-5-(4-hydroxyphenyl)-6-(4-(2-(piperidin-1-yl)ethoxy)phenyl)-7-oxabicyclo[2.2.1]hept-5-ene-2-sulfonate
[[Category: Unreleased Structures]]
[[Category: Sharma, N]]
[[Category: Nwachukwu, J.C]]
[[Category: Katzenellenbogen, J.A]]
[[Category: Srinivasan, S]]
[[Category: Carlson, K.E]]
[[Category: Sharma, A]]
[[Category: Nettles, K.W]]