
doi: 10.1038/nsmb.1400
pmid: 18270511
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.
Structure-Activity Relationship, Fluorescent Antibody Technique, Humans, Retinol-Binding Proteins, Cellular, DNA, Protein Serine-Threonine Kinases, Promoter Regions, Genetic, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Transcription Factors
Structure-Activity Relationship, Fluorescent Antibody Technique, Humans, Retinol-Binding Proteins, Cellular, DNA, Protein Serine-Threonine Kinases, Promoter Regions, Genetic, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Transcription Factors
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