Fig. 2: BIO-2007817 binds to the complex of parkin and pUb or pUbl. | Nature Communications

Fig. 2: BIO-2007817 binds to the complex of parkin and pUb or pUbl.

From: Activation of parkin by a molecular glue

Fig. 2

Isothermal titration calorimetry measurements with different parkin complexes and titrants (in italics). a BIO-2007817 binds to the R0RB:2×pUb complex with 150-fold higher affinity than the diastereomer BIO-2007818. b High-affinity binding requires the presence of pUb. c The K211N mutation in the RING0 pUb/pUbl-binding site prevents high-affinity binding. d BIO-2007817 also binds to the R0RB:pUbl complex. e Inclusion of ACT element with pUbl decreases the affinity of BIO-2007817 10-fold. f The F146Y mutation in RING0 ACT-binding site decreases the affinity 80-fold. g pUbl binds weakly to R0RB49,50. h Inclusion of BIO-2007817 increases the affinity of pUbl binding by 2400-fold. Protein concentrations and binding parameters are given in Supplementary Table 1.

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