6xzh: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 6xzh is ~~ON HOLD~~

==Structure of zVDR LBD-Calcitriol in complex with chimera 10==

== 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]] 2.372Å</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>

== 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.

~~Authors:~~ Buratto, J., ~~Belorusova~~, ~~A.Y.~~, Rochel, N., Guichard, G.

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>

~~Description: Structure~~ of ~~zVDR LBD~~-~~Calcitriol in complex with chimera 10~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: ~~Belorusova, A.Y~~]]

[[Category: ~~Guichard, G~~]]

[[Category: Buratto, J]]

==See Also==

[[Category: Rochel, N]]

*[[Vitamin D receptor 3D structures|Vitamin D receptor 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Danio rerio]]

[[Category: Large Structures]]

[[Category: Synthetic construct]]

[[Category: Belorusova AY]]

[[Category: Buratto J]]

[[Category: Guichard G]]

[[Category: Rochel N]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6xzh is ON HOLD
+==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.
-Authors: Buratto, J., Belorusova, A.Y., Rochel, N., Guichard, G.
+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>
-Description: Structure of zVDR LBD-Calcitriol in complex with chimera 10
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Belorusova, A.Y]]
+<div class="pdbe-citations 6xzh" style="background-color:#fffaf0;"></div>
-[[Category: Guichard, G]]
-[[Category: Buratto, J]]
+==See Also==
-[[Category: Rochel, N]]
+*[[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]]