8BV1
Peptide inhibitor P4 in complex with ASF1 histone chaperone
Summary for 8BV1
| Entry DOI | 10.2210/pdb8bv1/pdb |
| Descriptor | Histone chaperone ASF1A, P4 peptide inhibitor of histone chaperone ASF1, GLYCEROL, ... (4 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 | 117401.71 |
| Authors | Perrin, M.E.,Li, B.,Mbianda, J.,Ropars, V.,Legrand, P.,Douat, C.,Ochsenbein, F.,Guichard, G. (deposition date: 2022-12-01, release date: 2023-07-05, Last modification date: 2024-02-07) |
| 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: 37347155DOI: 10.1039/d3cc01891a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.834 Å) |
Structure validation
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