3kqi
crystal structure of PHF2 PHD domain complexed with H3K4Me3 peptidecrystal structure of PHF2 PHD domain complexed with H3K4Me3 peptide
Structural highlights
Function[PHF2_HUMAN] Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDistinct 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. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation.,Wen H, Li J, Song T, Lu M, Kan PY, Lee MG, Sha B, Shi X J Biol Chem. 2010 Mar 26;285(13):9322-6. Epub 2010 Feb 2. PMID:20129925[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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