1u3r

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{{STRUCTURE_1u3r| PDB=1u3r | SCENE= }}
 
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===Crystal Structure of Estrogen Receptor beta complexed with WAY-338===
 
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{{ABSTRACT_PUBMED_15456246}}
 
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==Function==
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==Crystal Structure of Estrogen Receptor beta complexed with WAY-338==
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[[http://www.uniprot.org/uniprot/ESR2_HUMAN ESR2_HUMAN]] Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA-binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual.
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<StructureSection load='1u3r' size='340' side='right'caption='[[1u3r]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1u3r]] 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=1U3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U3R FirstGlance]. <br>
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[[1u3r]] 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=1U3R OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=338:2-(5-HYDROXY-NAPHTHALEN-1-YL)-1,3-BENZOOXAZOL-6-OL'>338</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u3r OCA], [https://pdbe.org/1u3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u3r RCSB], [https://www.ebi.ac.uk/pdbsum/1u3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u3r ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ESR2_HUMAN ESR2_HUMAN] Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA-binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual.
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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/u3/1u3r_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/main_output.php?pdb_ID=1u3r ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Estrogen receptor|Estrogen receptor]]
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*[[Estrogen receptor 3D structures|Estrogen receptor 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:015456246</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Collini, M D.]]
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[[Category: Large Structures]]
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[[Category: Dinh, T.]]
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[[Category: Collini MD]]
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[[Category: Gunawan, I.]]
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[[Category: Dinh T]]
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[[Category: Harris, H A.]]
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[[Category: Gunawan I]]
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[[Category: Henderson, R A.]]
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[[Category: Harris HA]]
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[[Category: Keith, J C.]]
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[[Category: Henderson RA]]
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[[Category: Malamas, M S.]]
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[[Category: Keith Jr JC]]
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[[Category: Manas, E S.]]
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[[Category: Malamas MS]]
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[[Category: McDevitt, R E.]]
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[[Category: Manas ES]]
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[[Category: Miller, C P.]]
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[[Category: McDevitt RE]]
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[[Category: Xu, Z B.]]
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[[Category: Miller CP]]
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[[Category: Agonist]]
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[[Category: Xu ZB]]
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[[Category: Er]]
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[[Category: Er-beta]]
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[[Category: Estrogen]]
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[[Category: Estrogen receptor]]
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[[Category: Estrogen receptor beta]]
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[[Category: Nuclear receptor]]
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[[Category: Transcription]]
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[[Category: Transcription factor]]
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Current revision

Crystal Structure of Estrogen Receptor beta complexed with WAY-338

PDB ID 1u3r

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