View source for 8cj1


==Urea-based foldamer inhibitor c3u_3 chimera in complex with ASF1 histone chaperone==
<StructureSection load='8cj1' size='340' side='right'caption='[[8cj1]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8cj1]] is a 12 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=8CJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CJ1 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]] 2.564&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=66N:L-ALANINAMIDE'>66N</scene>, <scene name='pdbligand=URL:[(2~{S})-2-azanyl-4-methyl-pentyl]carbamic+acid'>URL</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=8cj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cj1 OCA], [https://pdbe.org/8cj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cj1 RCSB], [https://www.ebi.ac.uk/pdbsum/8cj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cj1 ProSAT]</span></td></tr>
</table>
== Function ==
[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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the search for foldamer inhibitors of the histone chaperone ASF1, we explored the possibility of substituting four alpha-residues ( approximately one helix turn) by 3-urea segments and scanned the sequence of a short alpha-helical peptide known to bind ASF1. By analysing the impact of the different foldamer replacements within the peptide chain, we uncovered new binding modes of the peptide-urea chimeras to ASF1.

Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach.,Perrin ME, Li B, Mbianda J, Bakail M, Andre C, Moal G, Legrand P, Ropars V, Douat C, Ochsenbein F, Guichard G Chem Commun (Camb). 2023 Jun 22. doi: 10.1039/d3cc01891a. PMID:37347155<ref>PMID:37347155</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8cj1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Douat C]]
[[Category: Guichard G]]
[[Category: Legrand P]]
[[Category: Li B]]
[[Category: Mbianda J]]
[[Category: Ochsenbein F]]
[[Category: Perrin ME]]
[[Category: Ropars V]]