Article
Peptide backbone conformation affects the substrate preference of protein arginine methyltransferase I.
Biochemistry - 10 Jul 2012
Kölbel Knut, Ihling Christian, Kühn Uwe, Neundorf Ines, Otto Silke, Stichel Jan, Robaa Dina, Beck-Sickinger Annette G, Sinz Andrea, Wahle Elmar
Abstract excerpt
Asymmetric dimethylation of arginine side chains is a common post-translational modification of eukaryotic proteins, which serves mostly to regulate protein-protein interactions. The modification is catalyzed by type I protein arginine methyltransferases, PRMT1 being the predominant member of the family. Determinants of substrate specificity of these enzymes are poorly understood. The Nuclear poly(A) binding...
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