Summary for 2K1J
| Entry DOI | 10.2210/pdb2k1j/pdb |
| Descriptor | Inhibitor of growth protein 4, ZINC ION (2 entities in total) |
| Functional Keywords | phd, zn, gene regulation, acetylation, alternative splicing, anti-oncogene, cell cycle, coiled coil, metal-binding, nucleus, zinc, zinc-finger |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q9UNL4 |
| Total number of polymer chains | 1 |
| Total formula weight | 7456.29 |
| Authors | Palacios, A.,Garcia, P.,Padro, D.,Lopez-Hernandez, E.,Blanco, F.J. (deposition date: 2008-03-05, release date: 2008-04-15, Last modification date: 2024-05-29) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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