1u3s: Difference between revisions

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{{STRUCTURE_1u3s|  PDB=1u3s  |  SCENE=  }}
===Crystal Structure of Estrogen Receptor beta complexed with WAY-797===
{{ABSTRACT_PUBMED_15456246}}


==Function==
==Crystal Structure of Estrogen Receptor beta complexed with WAY-797==
[[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.  
<StructureSection load='1u3s' size='340' side='right'caption='[[1u3s]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1u3s]] 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=1U3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U3S FirstGlance]. <br>
[[1u3s]] 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=1U3S OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=797:3-(6-HYDROXY-NAPHTHALEN-2-YL)-BENZO[D]ISOOXAZOL-6-OL'>797</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=1u3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u3s OCA], [https://pdbe.org/1u3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u3s RCSB], [https://www.ebi.ac.uk/pdbsum/1u3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u3s 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/u3/1u3s_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=1u3s ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Estrogen receptor|Estrogen receptor]]
*[[Estrogen receptor 3D structures|Estrogen receptor 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:015456246</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Collini, M D.]]
[[Category: Large Structures]]
[[Category: Dinh, T.]]
[[Category: Collini MD]]
[[Category: Gunawan, I.]]
[[Category: Dinh T]]
[[Category: Harris, H A.]]
[[Category: Gunawan I]]
[[Category: Henderson, R A.]]
[[Category: Harris HA]]
[[Category: Keith, J C.]]
[[Category: Henderson RA]]
[[Category: Malamas, M S.]]
[[Category: Keith Jr JC]]
[[Category: Manas, E S.]]
[[Category: Malamas MS]]
[[Category: McDevitt, R E.]]
[[Category: Manas ES]]
[[Category: Miller, C P.]]
[[Category: McDevitt RE]]
[[Category: Xu, Z B.]]
[[Category: Miller CP]]
[[Category: Agonist]]
[[Category: Xu ZB]]
[[Category: Er]]
[[Category: Er-beta]]
[[Category: Estrogen]]
[[Category: Estrogen receptor]]
[[Category: Estrogen receptor beta]]
[[Category: Nuclear receptor]]
[[Category: Transcription]]
[[Category: Transcription factor]]

Latest revision as of 11:43, 14 February 2024

Crystal Structure of Estrogen Receptor beta complexed with WAY-797Crystal Structure of Estrogen Receptor beta complexed with WAY-797

Structural highlights

1u3s is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1u3s, resolution 2.50Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA