1sj0

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[[Image:1sj0.png|left|200px]]
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==Human Estrogen Receptor Alpha Ligand-binding Domain in Complex with the Antagonist Ligand 4-D==
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<StructureSection load='1sj0' size='340' side='right' caption='[[1sj0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1sj0]] is a 1 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=1SJ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SJ0 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E4D:(2S,3R)-2-(4-(2-(PIPERIDIN-1-YL)ETHOXY)PHENYL)-2,3-DIHYDRO-3-(4-HYDROXYPHENYL)BENZO[B][1,4]OXATHIIN-6-OL'>E4D</scene><br>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ESR1, NR3A1, ESR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<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=1sj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sj0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1sj0 RCSB], [http://www.ebi.ac.uk/pdbsum/1sj0 PDBsum]</span></td></tr>
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<table>
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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/sj/1sj0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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 discovery and synthesis of dihydrobenzoxathiins as potent, ERalpha subtype selective ligands are described. The most active analogue, 4-D, was found to be 50-fold selective in a competitive binding assay and 100-fold selective in a transactivation assay in HEK-293 cells. The alpha selectivity was postulated to lie in the interaction of the sulfur atom of the benzoxathiin ring with the two discriminating residues in the binding pocket of the receptor isoforms.
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{{STRUCTURE_1sj0| PDB=1sj0 | SCENE= }}
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Estrogen receptor ligands. II. Discovery of benzoxathiins as potent, selective estrogen receptor alpha modulators.,Kim S, Wu JY, Birzin ET, Frisch K, Chan W, Pai LY, Yang YT, Mosley RT, Fitzgerald PM, Sharma N, Dahllund J, Thorsell AG, DiNinno F, Rohrer SP, Schaeffer JM, Hammond ML J Med Chem. 2004 Apr 22;47(9):2171-5. PMID:15084115<ref>PMID:15084115</ref>
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===Human Estrogen Receptor Alpha Ligand-binding Domain in Complex with the Antagonist Ligand 4-D===
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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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{{ABSTRACT_PUBMED_15084115}}
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==About this Structure==
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[[1sj0]] is a 1 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=1SJ0 OCA].
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==See Also==
==See Also==
*[[Estrogen receptor|Estrogen receptor]]
*[[Estrogen receptor|Estrogen receptor]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015084115</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Birzin, E T.]]
[[Category: Birzin, E T.]]

Revision as of 23:52, 28 September 2014

Human Estrogen Receptor Alpha Ligand-binding Domain in Complex with the Antagonist Ligand 4-D

1sj0, resolution 1.90Å

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