8CJ2

Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperone

Summary for 8CJ2

• Entry DOI: 10.2210/pdb8cj2/pdb
• Descriptor: Histone chaperone ASF1A, c3u_5 chimera inhibitor of histone chaperone ASF1, GLYCEROL, ... (5 entities in total)
• Functional Keywords: inhibitor, asf1, histone, protein-protein interaction, chaperone
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 8
• Total formula weight: 78171.68

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: 2024-07-10)

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

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

Experimental method

X-RAY DIFFRACTION (2.127 Å)