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TitleDistinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 15, Page 109-111, Year 2008
Publish dateJul 26, 2007 (structure data deposition date)
AuthorsLee, J. / Thompson, J.R. / Botuyan, M.V. / Mer, G.
External linksNat. Struct. Mol. Biol. / PubMed:18084306
MethodsX-ray diffraction
Resolution1.8 - 2.82 Å
Structure data

PDB-2qqr:
JMJD2A hybrid tudor domains
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2qqs:
JMJD2A tandem tudor domains in complex with a trimethylated histone H4-K20 peptide
Method: X-RAY DIFFRACTION / Resolution: 2.82 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / HISTONE LYSINE DEMETHYLASE / TANDEM HYBRID TUDOR DOMAINS / METAL BINDING PROTEIN / Chromatin regulator / Dioxygenase / Host-virus interaction / Iron / Metal-binding / Nucleus / Phosphorylation / Polymorphism / Transcription / Transcription regulation / Zinc / Zinc-finger / PROTEIN-METHYLATED PEPTIDE COMPLEX

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