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Fig. 3 | BMC Biology

Fig. 3

From: Identification of berberine as a novel drug for the treatment of multiple myeloma via targeting UHRF1

Fig. 3

BBR directly binds to UHRF1 in the TTD-PHD domain. a Structural overview of a UHRF1-BBR complex model predicted based on information from the competitive molecular docking experiment. There are three active sites in the UHRF1-BBR complex model. b Zoom-in view of the predicted active-site peptides (“IKWQDLEVGQV,” “MRRKSGPS,” and “PDNPKERGFWYD”). Key interface residues (D216, K297, and R235) in UHRF1 are shown. c Binding response curves of interactions between BBR and peptide 1/2/3. Peptide 3-BBR interaction was validated by surface plasmon resonance analysis. d Binding response curves of interactions between BBR and different domains of UHRF1 or hm-DNA. Proteins were purified from E. coli lysates overexpressing different domains of UHRF1. The BBR-UHRF1, BBR-TTD PHD domain, and BBR-hmDNA+UHRF1 interaction were validated by surface plasmon resonance analysis. e The average Kd values were measured in the surface plasmon resonance analysis. The data were presented as the mean ± SD obtained from three independent experiments

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