3KQI

crystal structure of PHF2 PHD domain complexed with H3K4Me3 peptide

Summary for 3KQI

• Entry DOI: 10.2210/pdb3kqi/pdb
• Descriptor: PHD finger protein 2, H3K4Me3 peptide, ZINC ION, ... (7 entities in total)
• Functional Keywords: phd finger, metal-binding, zinc-finger, histone-binding, nuclear protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 10233.44

Authors

Wen, H.,Li, J.Z.,Song, T.,Lu, M.,Lee, M. (deposition date: 2009-11-17, release date: 2010-02-02, Last modification date: 2019-02-13)

Primary citation

Wen, H.,Li, J.,Song, T.,Lu, M.,Kan, P.Y.,Lee, M.G.,Sha, B.,Shi, X.
Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation.
J.Biol.Chem., 285:9322-9326, 2010

PubMed Abstract: Distinct lysine methylation marks on histones create dynamic signatures deciphered by the "effector" modules, although the underlying mechanisms remain unclear. We identified the plant homeodomain- and Jumonji C domain-containing protein PHF2 as a novel histone H3K9 demethylase. We show in biochemical and crystallographic analyses that PHF2 recognizes histone H3K4 trimethylation through its plant homeodomain finger and that this interaction is essential for PHF2 occupancy and H3K9 demethylation at rDNA promoters. Our study provides molecular insights into the mechanism by which distinct effector domains within a protein cooperatively modulate the "cross-talk" of histone modifications.

PubMed: 20129925
DOI: 10.1074/jbc.C109.097667

Experimental method

X-RAY DIFFRACTION (1.78 Å)