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. Author manuscript; available in PMC: 2015 Jul 8.
Published in final edited form as: Nature. 2014 Oct 19;517(7533):223–226. doi: 10.1038/nature13826

Extended Data Figure 3. Both RNF146 RING and WWE domains contribute to iso-ADPr binding.

Extended Data Figure 3

a, Summary of iso-ADPr binding (Kd values) for RNF146(RING-WWE) obtained from the ITC titrations in the current work, and for the WWE-only fragment (previously published; indicated by asterisk)13. These data indicate that the RING domain contributes to iso-ADPr binding. b, Raw ITC titrations of RNF146(RING-WWE) fragments: (left to right) WT, K61A, and K61D. c, Limited proteolysis of RNF146(RING-WWE) and of a construct of RNF146 including the linker between the RING and WWE domains, and the WWE domain (RNF146(Linker-WWE); residues 83–183). Both appear to result in the same product when treated with subtilisin. The RING-WWE construct is more resistant to subtilisin in the presence of ligand.