2QQR
JMJD2A hybrid tudor domains
Summary for 2QQR
| Entry DOI | 10.2210/pdb2qqr/pdb |
| Related | 2QQS |
| Descriptor | JmjC domain-containing histone demethylation protein 3A, SULFATE ION (3 entities in total) |
| Functional Keywords | histone lysine demethylase, tandem hybrid tudor domains, metal binding protein, chromatin regulator, dioxygenase, host-virus interaction, iron, metal-binding, nucleus, oxidoreductase, phosphorylation, polymorphism, transcription, transcription regulation, zinc, zinc-finger |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: O75164 |
| Total number of polymer chains | 2 |
| Total formula weight | 27675.59 |
| Authors | Lee, J.,Botuyan, M.V.,Mer, G. (deposition date: 2007-07-26, release date: 2007-12-11, Last modification date: 2024-11-06) |
| Primary citation | Lee, J.,Thompson, J.R.,Botuyan, M.V.,Mer, G. Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Nat.Struct.Mol.Biol., 15:109-111, 2008 Cited by PubMed Abstract: The lysine demethylase JMJD2A has the unique property of binding trimethylated peptides from two different histone sequences (H3K4me3 and H4K20me3) through its tudor domains. Here we show using X-ray crystallography and calorimetry that H3K4me3 and H4K20me3, which are recognized with similar affinities by JMJD2A, adopt radically different binding modes, to the extent that we were able to design single point mutations in JMJD2A that inhibited the recognition of H3K4me3 but not H4K20me3 and vice versa. PubMed: 18084306DOI: 10.1038/nsmb1326 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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