2QQS

JMJD2A tandem tudor domains in complex with a trimethylated histone H4-K20 peptide

Summary for 2QQS

• Entry DOI: 10.2210/pdb2qqs/pdb
• Related: 2QQR
• Descriptor: JmjC domain-containing histone demethylation protein 3A, METHYLATED HISTONE H4 PEPTIDE (3 entities in total)
• Functional Keywords: histone lysine demethylase, metal binding protein, protein-methylated peptide complex, chromatin regulator, dioxygenase, host-virus interaction, iron, metal-binding, nucleus, oxidoreductase, phosphorylation, polymorphism, transcription, transcription regulation, zinc, zinc-finger
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: O75164
• Total number of polymer chains: 4
• Total formula weight: 29650.96

Authors

Lee, J.,Botuyan, M.V.,Mer, G. (deposition date: 2007-07-26, release date: 2007-12-11, Last modification date: 2023-08-30)

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

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: 18084306
DOI: 10.1038/nsmb1326

Experimental method

X-RAY DIFFRACTION (2.82 Å)