8cj3

Urea-based foldamer inhibitor c3u_7 chimera in complex with ASF1 histone chaperone

spinqualitylabelsall models 8cj3, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cj3 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: ACE, ALN, NH2, OUI, OUR, QQ8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. 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 Jul 11;59(56):8696-8699. doi: 10.1039/d3cc01891a. PMID:37347155 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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