2yjd

From Proteopedia

(Difference between revisions)

Revision as of 10:10, 22 June 2022

Stapled peptide bound to Estrogen Receptor Beta

Structural highlights

2yjd is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:	, ,
Related:	2yly, 1l2j, 2fsz, 1x7b, 1x76, 1nde, 2jj3, 1yy4, 1u3s, 1x78, 1qkm, 1u3r, 1x7j, 1u9e, 1yye, 1u3q, 2yja, 2ldd, 2lda, 2ldc
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.

Publication Abstract from PubMed

Synthetic 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.

References

↑ 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. Design and structure of stapled peptides binding to estrogen receptors. J Am Chem Soc. 2011 Jun 29;133(25):9696-9. Epub 2011 Jun 6. PMID:21612236 doi:10.1021/ja202946k

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2yjd"

@@ Line 3: / Line 3: @@
 <StructureSection load='2yjd' size='340' side='right'caption='[[2yjd]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2yjd]] is a 4 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=2YJD FirstGlance]. <br>
+<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>
 <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'>[http://proteopedia.org/fgij/fg.htm?mol=2yjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yjd OCA], [http://pdbe.org/2yjd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yjd RCSB], [http://www.ebi.ac.uk/pdbsum/2yjd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yjd ProSAT]</span></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=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>
 == Function ==
-[[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.
+[[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;">
 == Publication Abstract from PubMed ==

2yjd

From Proteopedia

Revision as of 10:10, 22 June 2022

Stapled peptide bound to Estrogen Receptor Beta

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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Proteopedia Page Contributors and Editors (what is this?)

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