2yjd: Difference between revisions
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<StructureSection load='2yjd' size='340' side='right'caption='[[2yjd]], [[Resolution|resolution]] 1.93Å' scene=''> | <StructureSection load='2yjd' size='340' side='right'caption='[[2yjd]], [[Resolution|resolution]] 1.93Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yjd]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2yjd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YJD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=YJD:4-(2-PROPAN-2-YLOXYBENZIMIDAZOL-1-YL)PHENOL'>YJD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=YJD:4-(2-PROPAN-2-YLOXYBENZIMIDAZOL-1-YL)PHENOL'>YJD</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MK8:2-METHYL-L-NORLEUCINE'>MK8</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MK8:2-METHYL-L-NORLEUCINE'>MK8</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yly|2yly]], [[1l2j|1l2j]], [[2fsz|2fsz]], [[1x7b|1x7b]], [[1x76|1x76]], [[1nde|1nde]], [[2jj3|2jj3]], [[1yy4|1yy4]], [[1u3s|1u3s]], [[1x78|1x78]], [[1qkm|1qkm]], [[1u3r|1u3r]], [[1x7j|1x7j]], [[1u9e|1u9e]], [[1yye|1yye]], [[1u3q|1u3q]], [[2yja|2yja]], [[2ldd|2ldd]], [[2lda|2lda]], [[2ldc|2ldc]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2yly|2yly]], [[1l2j|1l2j]], [[2fsz|2fsz]], [[1x7b|1x7b]], [[1x76|1x76]], [[1nde|1nde]], [[2jj3|2jj3]], [[1yy4|1yy4]], [[1u3s|1u3s]], [[1x78|1x78]], [[1qkm|1qkm]], [[1u3r|1u3r]], [[1x7j|1x7j]], [[1u9e|1u9e]], [[1yye|1yye]], [[1u3q|1u3q]], [[2yja|2yja]], [[2ldd|2ldd]], [[2lda|2lda]], [[2ldc|2ldc]]</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=2yjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yjd OCA], [https://pdbe.org/2yjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yjd RCSB], [https://www.ebi.ac.uk/pdbsum/2yjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yjd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 13:10, 22 June 2022
Stapled peptide bound to Estrogen Receptor BetaStapled peptide bound to Estrogen Receptor Beta
Structural highlights
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. Publication Abstract from PubMedSynthetic peptides that specifically bind nuclear hormone receptors offer an alternative approach to small molecules for the modulation of receptor signaling and subsequent gene expression. Here we describe the design of a series of novel stapled peptides that bind the coactivator peptide site of estrogen receptors. Using a number of biophysical techniques, including crystal structure analysis of receptor-stapled peptide complexes, we describe in detail the molecular interactions and demonstrate that all-hydrocarbon staples modulate molecular recognition events. The findings have implications for the design of stapled peptides in general. Design and structure of stapled peptides binding to estrogen receptors.,Phillips C, Roberts LR, Schade M, Bazin R, Bent A, Davies NL, Moore R, Pannifer AD, Pickford AR, Prior SH, Read CM, Scott A, Brown DG, Xu B, Irving SL J Am Chem Soc. 2011 Jun 29;133(25):9696-9. Epub 2011 Jun 6. PMID:21612236[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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