6zuf

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Current revision (10:54, 15 November 2023) (edit) (undo)
 
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==Urea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperone==
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<StructureSection load='6zuf' size='340' side='right'caption='[[6zuf]]' scene=''>
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<StructureSection load='6zuf' size='340' side='right'caption='[[6zuf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6zuf]] 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=6ZUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZUF FirstGlance]. <br>
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</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=6zuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zuf OCA], [https://pdbe.org/6zuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zuf RCSB], [https://www.ebi.ac.uk/pdbsum/6zuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zuf ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.798&#8491;</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OUR:[AZANYL-[[(4~{S})-4-AZANYL-5-(CARBOXYAMINO)PENTYL]AMINO]METHYLIDENE]AZANIUM'>OUR</scene>, <scene name='pdbligand=QQ8:(4~{S})-4-azanyl-5-formamido-pentanamide'>QQ8</scene>, <scene name='pdbligand=QQB:~{N}-[(2~{S})-2-azanyl-3-naphthalen-1-yl-propyl]methanamide'>QQB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=URL:[(2~{S})-2-azanyl-4-methyl-pentyl]carbamic+acid'>URL</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=6zuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zuf OCA], [https://pdbe.org/6zuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zuf RCSB], [https://www.ebi.ac.uk/pdbsum/6zuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zuf ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ASF1A_HUMAN ASF1A_HUMAN] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.<ref>PMID:10759893</ref> <ref>PMID:11897662</ref> <ref>PMID:12842904</ref> <ref>PMID:14718166</ref> <ref>PMID:15621527</ref> <ref>PMID:16151251</ref> <ref>PMID:15664198</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Sequence-specific oligomers with predictable folding patterns, i.e., foldamers, provide new opportunities to mimic alpha-helical peptides and design inhibitors of protein-protein interactions. One major hurdle of this strategy is to retain the correct orientation of key side chains involved in protein surface recognition. Here, we show that the structural plasticity of a foldamer backbone may notably contribute to the required spatial adjustment for optimal interaction with the protein surface. By using oligoureas as alpha helix mimics, we designed a foldamer/peptide hybrid inhibitor of histone chaperone ASF1, a key regulator of chromatin dynamics. The crystal structure of its complex with ASF1 reveals a notable plasticity of the urea backbone, which adapts to the ASF1 surface to maintain the same binding interface. One additional benefit of generating ASF1 ligands with nonpeptide oligourea segments is the resistance to proteolysis in human plasma, which was highly improved compared to the cognate alpha-helical peptide.
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Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity.,Mbianda J, Bakail M, Andre C, Moal G, Perrin ME, Pinna G, Guerois R, Becher F, Legrand P, Traore S, Douat C, Guichard G, Ochsenbein F Sci Adv. 2021 Mar 19;7(12):eabd9153. doi: 10.1126/sciadv.abd9153. Print 2021 Mar. PMID:33741589<ref>PMID:33741589</ref>
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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 6zuf" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Bakail M]]
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[[Category: Douat C]]
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[[Category: Guerois R]]
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[[Category: Guichard G]]
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[[Category: Legrand P]]
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[[Category: Mbianda J]]
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[[Category: Ochsenbein F]]
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[[Category: Perrin EM]]
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[[Category: Traore S]]

Current revision

Urea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperone

PDB ID 6zuf

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