2yjd: Difference between revisions
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New page: '''Unreleased structure''' The entry 2yjd is ON HOLD until sometime in the future Authors: Phillips, C., Roberts, L.R., Schade, M., Bent, A., Davies, N.L., Moore, R., Pannifer, A.D., Br... |
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==Stapled peptide bound to Estrogen Receptor Beta== | |||
<StructureSection load='2yjd' size='340' side='right'caption='[[2yjd]], [[Resolution|resolution]] 1.93Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2yjd]] 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>, <scene name='pdbligand=YJD:4-(2-PROPAN-2-YLOXYBENZIMIDAZOL-1-YL)PHENOL'>YJD</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=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> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:21612236</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2yjd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Estrogen receptor 3D structures|Estrogen receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Bent A]] | |||
[[Category: Brown DG]] | |||
[[Category: Davies NL]] | |||
[[Category: Irving SL]] | |||
[[Category: Moore R]] | |||
[[Category: Pannifer AD]] | |||
[[Category: Phillips C]] | |||
[[Category: Pickford AR]] | |||
[[Category: Roberts LR]] | |||
[[Category: Schade M]] | |||
Latest revision as of 04:32, 21 November 2024
Stapled peptide bound to Estrogen Receptor BetaStapled peptide bound to Estrogen Receptor Beta
Structural highlights
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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