2K1J の概要
| エントリーDOI | 10.2210/pdb2k1j/pdb |
| 分子名称 | Inhibitor of growth protein 4, ZINC ION (2 entities in total) |
| 機能のキーワード | phd, zn, gene regulation, acetylation, alternative splicing, anti-oncogene, cell cycle, coiled coil, metal-binding, nucleus, zinc, zinc-finger |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Nucleus: Q9UNL4 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 7456.29 |
| 構造登録者 | Palacios, A.,Garcia, P.,Padro, D.,Lopez-Hernandez, E.,Blanco, F.J. (登録日: 2008-03-05, 公開日: 2008-04-15, 最終更新日: 2024-05-29) |
| 主引用文献 | Palacios, A.,Garcia, P.,Padro, D.,Lopez-Hernandez, E.,Martin, I.,Blanco, F.J. Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4. Febs Lett., 580:6903-6908, 2006 Cited by PubMed Abstract: Plant homeodomain (PHD) fingers are frequently present in proteins involved in chromatin remodelling, and some of them bind to histones. The family of proteins inhibitors of growth (ING) contains a PHD finger that bind to histone-3 trimethylated at lysine 4, and those of ING1 and ING2 also act as nuclear phosphoinositide receptors. We have determined the structure of ING4 PHD, and characterised its binding to phosphoinositides and histone methylated tails. In contrast to ING2, ING4 is not a phosphoinositide receptor and binds with similar affinity to the different methylation states of histone-3 at lysine 4. PubMed: 17157298DOI: 10.1016/j.febslet.2006.11.055 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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