Fig. 2: Allosteric di-Ub enhances UbcH7-Ub binding affinity for HOIL-1 and RNF216.
From: The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family
a Representative isothermal titration calorimetry (ITC) of isopeptide linked UbcH7(C86K)-Ub conjugate titrated into HOIL-1 helix-RBR (C460A) in the absence or presence of different di-Ub linkages. b ITC of isopeptide linked UbcH7(C86K)-Ub conjugate titrated into RNF216 RBR-helix (C688A, pSer719) in the absence or presence of different di-Ub linkages. c Summary of ITC experiment statistics. The titration of UbcH7-Ub into HOIL-1/M1 di-Ub was performed in duplicate, and statistics for both individual experiments are provided.
