2lda

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'''Unreleased structure'''
 
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The entry 2lda is ON HOLD until Paper Publication
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==Solution structure of the estrogen receptor-binding stapled peptide SP2 (Ac-HKXLHQXLQDS-NH2)==
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<StructureSection load='2lda' size='340' side='right'caption='[[2lda]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2lda]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LDA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr>
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<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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lda OCA], [https://pdbe.org/2lda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lda RCSB], [https://www.ebi.ac.uk/pdbsum/2lda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lda ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Phillips, C., Bazin, R., Bent, A., Davies, N., Moore, R., Pannifer, A., Pickford, A., Prior, S., Read, C., Roberts, L., Schade, M., Scott, A., Brown, D., Xu, B., Irving, S.
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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>
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Description: Solution structure of the estrogen receptor-binding stapled peptide SP2 (Ac-HKXLHQXLQDS-NH2)
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2lda" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Bazin R]]
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[[Category: Bent A]]
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[[Category: Brown D]]
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[[Category: Davies N]]
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[[Category: Irving S]]
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[[Category: Moore R]]
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[[Category: Pannifer A]]
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[[Category: Phillips C]]
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[[Category: Pickford A]]
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[[Category: Prior S]]
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[[Category: Read C]]
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[[Category: Roberts L]]
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[[Category: Schade M]]
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[[Category: Scott A]]
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[[Category: Xu B]]

Current revision

Solution structure of the estrogen receptor-binding stapled peptide SP2 (Ac-HKXLHQXLQDS-NH2)

PDB ID 2lda

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