1x7j: Difference between revisions

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-[[Image:1x7j.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF ESTROGEN RECEPTOR BETA COMPLEXED WITH GENISTEIN==
-|PDB= 1x7j |SIZE=350|CAPTION= <scene name='initialview01'>1x7j</scene>, resolution 2.30&Aring;
+<StructureSection load='1x7j' size='340' side='right'caption='[[1x7j]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=GEN:GENISTEIN'>GEN</scene>
+<table><tr><td colspan='2'>[[1x7j]] 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=1X7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X7J FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-|GENE= ESR2, NR3A2, ESTRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GEN:GENISTEIN'>GEN</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=1x7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7j OCA], [https://pdbe.org/1x7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x7j RCSB], [https://www.ebi.ac.uk/pdbsum/1x7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x7j ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+== 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/x7/1x7j_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/main_output.php?pdb_ID=1x7j ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF ESTROGEN RECEPTOR BETA COMPLEXED WITH GENISTEIN'''
+==See Also==
+*[[Estrogen receptor 3D structures|Estrogen receptor 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-We present X-ray crystallographic and molecular modeling studies of estrogen receptors-alpha and -beta complexed with the estrogen receptor-beta-selective phytoestrogen genistein, and coactivator-derived NR box peptides containing an LXXLL motif. We demonstrate that the ligand binding mode is essentially identical when genistein is bound to both isoforms, despite the considerably weaker affinity of this ligand for estrogen receptor-alpha. In addition, we examine subtle differences between binding site residues, providing an explanation for why genistein is modestly selective for the beta isoform. To this end, we also present the results of quantum chemical studies and thermodynamic arguments that yield insight to the nature of the interactions leading to estrogen receptor-beta selectivity. The importance of our analysis to structure-based drug design is discussed.
-==About this Structure==
-X7J is a [[Single protein]] structure of 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=1X7J OCA].
-==Reference==
-Understanding the selectivity of genistein for human estrogen receptor-beta using X-ray crystallography and computational methods., Manas ES, Xu ZB, Unwalla RJ, Somers WS, Structure. 2004 Dec;12(12):2197-207. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15576033 15576033]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Manas, E S.]]
+[[Category: Manas ES]]
-[[Category: Somers, W S.]]
+[[Category: Somers WS]]
-[[Category: Unwalla, R J.]]
+[[Category: Unwalla RJ]]
-[[Category: Xu, Z B.]]
+[[Category: Xu ZB]]
-[[Category: GEN]]
-[[Category: agonist]]
-[[Category: er]]
-[[Category: er-beta]]
-[[Category: estrogen]]
-[[Category: estrogen receptor]]
-[[Category: estrogen receptor beta]]
-[[Category: nuclear receptor]]
-[[Category: transcription factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:06:05 2008''