2j7x
From Proteopedia
(Difference between revisions)
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<StructureSection load='2j7x' size='340' side='right'caption='[[2j7x]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2j7x' size='340' side='right'caption='[[2j7x]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2j7x]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2j7x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J7X FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EST:ESTRADIOL'>EST</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EST:ESTRADIOL'>EST</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hj1|1hj1]], [[1qkn|1qkn]], [[1v95|1v95]], [[2j7y|2j7y]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hj1|1hj1]], [[1qkn|1qkn]], [[1v95|1v95]], [[2j7y|2j7y]]</div></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j7x OCA], [https://pdbe.org/2j7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j7x RCSB], [https://www.ebi.ac.uk/pdbsum/2j7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j7x ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/ESR2_RAT ESR2_RAT]] Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform 3 and isoform 4 are unable to bind DNA and activate transcription due to the truncation of the DNA binding domain. Isoform 2 shows loss of ligand binding affinity and suppresses ER-alpha and ER-beta1 mediated transcriptional activation and may act as a dominant negative regulator of estrogen action. [[https://www.uniprot.org/uniprot/NCOA5_HUMAN NCOA5_HUMAN]] Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2).<ref>PMID:15073177</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 08:03, 19 January 2022
STRUCTURE OF ESTRADIOL-BOUND ESTROGEN RECEPTOR BETA LBD IN COMPLEX WITH LXXLL MOTIF FROM NCOA5
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Categories: Buffalo rat | Large Structures | Bonn, T | Brzozowski, A M | Carlquist, M | Engstrom, O | Gustaffson, J A | Hubbard, R E | Ljunggren, J | Pike, A C.W | Thorsell, A G | Walton, J | Glycoprotein | Nuclear receptor | Phosphorylation | Steroid-binding | Transcription | Transcription regulation | Zinc-finger