View source for 6xzh


==Structure of zVDR LBD-Calcitriol in complex with chimera 10==
<StructureSection load='6xzh' size='340' side='right'caption='[[6xzh]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xzh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XZH 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]] 2.372&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OUK:[(5~{S})-5-AZANYL-6-(CARBOXYAMINO)HEXYL]AZANIUM'>OUK</scene>, <scene name='pdbligand=URL:[(2~{S})-2-azanyl-4-methyl-pentyl]carbamic+acid'>URL</scene>, <scene name='pdbligand=VDX:5-{2-[1-(5-HYDROXY-1,5-DIMETHYL-HEXYL)-7A-METHYL-OCTAHYDRO-INDEN-4-YLIDENE]-ETHYLIDENE}-4-METHYLENE-CYCLOHEXANE-1,3-DIOL'>VDX</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=6xzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xzh OCA], [https://pdbe.org/6xzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xzh RCSB], [https://www.ebi.ac.uk/pdbsum/6xzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xzh ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Efficient optimization of a peptide lead into a drug candidate frequently needs further transformation to augment properties such as bioavailability. Among the different options, foldamers, which are sequence-based oligomers with precise folded conformation, have emerged as a promising technology. We introduce oligourea foldamers to reduce the peptide character of inhibitors of protein-protein interactions (PPI). However, the precise design of such mimics is currently limited by the lack of structural information on how these foldamers adapt to protein surfaces. We report a collection of X-ray structures of peptide-oligourea hybrids in complex with ubiquitin ligase MDM2 and vitamin D receptor and show how such hybrid oligomers can be designed to bind with high affinity to protein targets. This work should enable the generation of more effective foldamer-based disruptors of PPIs in the context of peptide lead optimization.

Structural Basis for alpha-Helix Mimicry and Inhibition of Protein-Protein Interactions with Oligourea Foldamers.,Cussol L, Mauran-Ambrosino L, Buratto J, Belorusova AY, Neuville M, Osz J, Fribourg S, Fremaux J, Dolain C, Goudreau SR, Rochel N, Guichard G Angew Chem Int Ed Engl. 2020 Sep 16. doi: 10.1002/anie.202008992. PMID:32935897<ref>PMID:32935897</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xzh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Vitamin D receptor 3D structures|Vitamin D receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Danio rerio]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Belorusova AY]]
[[Category: Buratto J]]
[[Category: Guichard G]]
[[Category: Rochel N]]