Correction: Structural insights into the nanomolar affinity of RING E3 ligase ZNRF1 for Ube2N and its functional implications

Biochem. J. (2018) 475, 1569–1582; DOI: 10.1042/BCJ20170909

The authors have become aware of an error in one of their figures they would like to correct. The ITC thermogram in Figure 3C was duplicated in Figure 3D, Figure 3E displayed the ITC thermogram for Figure 3D and the ITC thermogram for Figure 3E was omitted. The correct version of Figure 3 is below. The authors apologize for this error. The authors note that this correction neither changes any of the conclusions derived out of them nor any of the binding parameters reported in the article as they were correctly represented in the text and table 2.

Figure 3. Contribution of Arg14^Ube2N : Glu183^ZNRF1 H-bond/salt-bridge interaction in ZNRF1 : Ube2N affinity.

(A) A close up of ZNRF1^CTD (in blue) : Ube2N (in red) interface depicting the H-bonding network involving Arg14, Lys10, and Arg6 of Ube2N with Glu183, Leu188, and Glu189 of ZNRF1. H-bonding distances are also indicated. (B–E) Binding isotherms of ZNRF1^CTD to Ube2D2^D12R (B), Ube2N^R14D (C), Ube2N^R14A (D), and that of ZNRF1^{CTD, E183A} to wtUbe2N (E) at 25°C. Titrations and data analyses were carried out as in Figure 1. (F) ZNRF1^CTD and Ube2N also interact via water molecules forming an extensive network of H-bonds (shown with dotted lines). H-bonding distances are also mentioned. B-factors of the water molecules and that of the protein atoms are comparable illustrating their importance.