1KNE
Chromo domain of HP1 complexed with histone H3 tail containing trimethyllysine 9
Summary for 1KNE
| Entry DOI | 10.2210/pdb1kne/pdb |
| Related | 1KNA |
| Descriptor | HETEROCHROMATIN PROTEIN 1, Trimethylated Histone H3 (3 entities in total) |
| Functional Keywords | chromo, hp1, histone, trimethyllysine, methyllysine, h3, chromatin, structural protein |
| Biological source | Drosophila melanogaster (fruit fly) More |
| Cellular location | Nucleus: P05205 Nucleus (By similarity): P02299 |
| Total number of polymer chains | 2 |
| Total formula weight | 10357.52 |
| Authors | Jacobs, S.A.,Khorasanizadeh, S. (deposition date: 2001-12-18, release date: 2002-03-20, Last modification date: 2021-10-27) |
| Primary citation | Jacobs, S.A.,Khorasanizadeh, S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science, 295:2080-2083, 2002 Cited by PubMed Abstract: The chromodomain of the HP1 family of proteins recognizes histone tails with specifically methylated lysines. Here, we present structural, energetic, and mutational analyses of the complex between the Drosophila HP1 chromodomain and the histone H3 tail with a methyllysine at residue 9, a modification associated with epigenetic silencing. The histone tail inserts as a beta strand, completing the beta-sandwich architecture of the chromodomain. The methylammonium group is caged by three aromatic side chains, whereas adjacent residues form discerning contacts with one face of the chromodomain. Comparison of dimethyl- and trimethyllysine-containing complexes suggests a role for cation-pi and van der Waals interactions, with trimethylation slightly improving the binding affinity. PubMed: 11859155DOI: 10.1126/science.1069473 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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