8CJ1

Urea-based foldamer inhibitor c3u_3 chimera in complex with ASF1 histone chaperone

Summary for 8CJ1

Entry DOI	10.2210/pdb8cj1/pdb
Descriptor	Histone chaperone ASF1A, c3u_3 chimera inhibitor of histone chaperone ASF1 (3 entities in total)
Functional Keywords	inhibitor, asf1, histone, protein-protein interaction, chaperone
Biological source	Homo sapiens (human) More
Total number of polymer chains	12
Total formula weight	146339.70
Authors	Perrin, M.E.,Li, B.,Mbianda, J.,Ropars, V.,Legrand, P.,Douat, C.,Ochsenbein, F.,Guichard, G. (deposition date: 2023-02-11, release date: 2023-07-05, Last modification date: 2023-11-15)
Primary citation	Perrin, M.E.,Li, B.,Mbianda, J.,Bakail, M.,Andre, C.,Moal, G.,Legrand, P.,Ropars, V.,Douat, C.,Ochsenbein, F.,Guichard, G. Unexpected binding modes of inhibitors to the histone chaperone ASF1 revealed by a foldamer scanning approach. Chem.Commun.(Camb.), 59:8696-8699, 2023 Cited by PubMed Abstract: In the search for foldamer inhibitors of the histone chaperone ASF1, we explored the possibility of substituting four α-residues (≈one helix turn) by 3-urea segments and scanned the sequence of a short α-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. PubMed: 37347155 DOI: 10.1039/d3cc01891a PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.564 Å)

Structure validation