8CJ2
Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperone
8CJ2 の概要
| エントリーDOI | 10.2210/pdb8cj2/pdb |
| 分子名称 | Histone chaperone ASF1A, c3u_5 chimera inhibitor of histone chaperone ASF1, GLYCEROL, ... (5 entities in total) |
| 機能のキーワード | inhibitor, asf1, histone, protein-protein interaction, chaperone |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 78171.68 |
| 構造登録者 | Perrin, M.E.,Li, B.,Mbianda, J.,Ropars, V.,Legrand, P.,Douat, C.,Ochsenbein, F.,Guichard, G. (登録日: 2023-02-11, 公開日: 2023-07-05, 最終更新日: 2024-07-10) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.127 Å) |
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