Epitopes described in "Interaction of JMJD6 with single-stranded RNA."

Reference
Article Authors:Xia Hong; Jianye Zang; Janice White; Chao Wang; Cheol-Ho Pan; Rui Zhao; Robert C Murphy; Shaodong Dai; Peter Henson; John W Kappler; James Hagman; Gongyi Zhang
Article Title:Interaction of JMJD6 with single-stranded RNA.
Reference Detail
Reference ID:1024875
Abstract:JMJD6 is a Jumonji C domain-containing hydroxylase. JMJD6 binds alpha-ketoglutarate and iron and has been characterized as either a histone arginine demethylase or U2AF65 lysyl hydroxylase. Here, we describe the structures of JMJD6 with and without alpha-ketoglutarate, which revealed a novel substrate binding groove and two positively charged surfaces. The structures also contain a stack of aromatic residues located near the active center. The side chain of one residue within this stack assumed different conformations in the two structures. Interestingly, JMJD6 bound efficiently to single-stranded RNA, but not to single-stranded DNA, double-stranded RNA, or double-stranded DNA. These structural features and truncation analysis of JMJD6 suggest that JMJD6 may bind and modify single-stand RNA rather than the previously reported peptide substrates.
Date:2010
Reference Type:Literature
PubMed ID:20679243
Journal:Proc Natl Acad Sci U S A
Journal Volume:107
Article Pages:14568-72
Journal ISSN:1091-6490
Article Chemical List:DNA, Single-Stranded;RNA, Double-Stranded;RNA;DNA;Jumonji Domain-Containing Histone Demethylases;KDM6B protein, human
Article MeSH List:Binding Sites(genetics); Binding, Competitive; DNA(chemistry; metabolism); DNA, Single-Stranded(chemistry; metabolism); Electrophoretic Mobility Shift Assay; Humans; Jumonji Domain-Containing Histone Demethylases(chemistry; genetics; metabolism); Models, Molecular; Nucleic Acid Conformation; Protein Binding; Protein Structure, Tertiary; RNA(chemistry; metabolism); RNA, Double-Stranded(chemistry; metabolism); Substrate Specificity
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