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2JXJ

NMR structure of the ARID domain from the histone H3K4 demethylase RBP2

Summary for 2JXJ
Entry DOI10.2210/pdb2jxj/pdb
DescriptorHistone demethylase JARID1A (1 entity in total)
Functional Keywordsarid domain, chromatin regulator, developmental protein, dioxygenase, iron, metal-binding, nucleus, oxidoreductase, phosphoprotein, polymorphism, transcription, transcription regulation, zinc, zinc-finger
Biological sourceHomo sapiens (Human)
Cellular locationNucleus, nucleolus: P29375
Total number of polymer chains1
Total formula weight10836.68
Authors
Tu, S.,Yuan, C.,Tsai, M. (deposition date: 2007-11-20, release date: 2008-09-30, Last modification date: 2024-05-29)
Primary citationTu, S.,Teng, Y.C.,Yuan, C.,Wu, Y.T.,Chan, M.Y.,Cheng, A.N.,Lin, P.H.,Juan, L.J.,Tsai, M.D.
The ARID domain of the H3K4 demethylase RBP2 binds to a DNA CCGCCC motif
Nat.Struct.Mol.Biol., 15:419-421, 2008
Cited by
PubMed Abstract: The histone H3 lysine 4 demethylase RBP2 contains a DNA binding domain, the AT-rich interaction domain (ARID). We solved the structure of ARID by NMR, identified its DNA binding motif (CCGCCC) and characterized the binding contacts. Immunofluorescence and luciferase assays indicated that ARID is required for RBP2 demethylase activity in cells and that DNA recognition is essential to regulate transcription.
PubMed: 18270511
DOI: 10.1038/nsmb.1400
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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