3ols
From Proteopedia
(Difference between revisions)
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | {{Seed}} | ||
| - | [[Image:3ols.jpg|left|200px]] | ||
| - | < | + | ==Crystal structure of estrogen receptor beta ligand binding domain== |
| - | + | <StructureSection load='3ols' size='340' side='right'caption='[[3ols]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | or the | + | <table><tr><td colspan='2'>[[3ols]] 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=3OLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OLS FirstGlance]. <br> |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EST:ESTRADIOL'>EST</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=3ols FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ols OCA], [https://pdbe.org/3ols PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ols RCSB], [https://www.ebi.ac.uk/pdbsum/3ols PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ols 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. | ||
| - | == | + | ==See Also== |
| - | + | *[[Estrogen receptor 3D structures|Estrogen receptor 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Brunsveld | + | [[Category: Large Structures]] |
| - | [[Category: Carraz | + | [[Category: Brunsveld L]] |
| - | [[Category: Moecklinghoff | + | [[Category: Carraz M]] |
| - | [[Category: Ottmann | + | [[Category: Moecklinghoff S]] |
| - | [[Category: Rose | + | [[Category: Ottmann C]] |
| - | [[Category: Visser | + | [[Category: Rose R]] |
| - | + | [[Category: Visser A]] | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal structure of estrogen receptor beta ligand binding domain
| |||||||||||
