Novel Insights into Peptide Binding and Conformational Dynamics of UHRF1

In this issue of Structure, Kori et al. (2019) Kori S. Ferry L. Matano S. Jimenji T. Kodera N. Tsusaka T. Matsumura R. Oda T. Sato M. Dohmae N. et al. Structure of the UHRF1 Tandem Tudor Domain bound to a methylated non-histone protein, LIG1, reveals rules for binding and regulation. Structure. 2019; 27 ( this issue) : 485-496 Google Scholar report the crystal structure of a lysine-methylated non-histone peptide from DNA ligase 1 (LIG1K126me3) bound to the UHRF1 tandem Tudor domain (TTD). LIG1K126me3-TTD exhibits strong interactions involving peptide residues K120 to K126me3, regulated by phosphorylation, which affects the conformation of UHRF1