Fig. 6: Influence of inhibitors on BiP-Grp94-client ternary complex.
From: Mechanism of client loading from BiP to Grp94 and its disruption by select inhibitors
A FP of FITC-labeled proIGF225-120 with varying concentrations of BiP (red), Grp94 (blue), and BiP and Grp94 (green) under ADP conditions. Solid lines for BiP (KD = 1.5 ± 0.7 μM) and BiP/Grp94 (KD,app = 1.1 ± 0.2 μM) are fits to a single-site binding equation. Grp94 only data is a linear fit. Double-headed arrow represents increase in polarization due to Grp94 association. Yellow circle with F represents labeling site of FITC on proIGF225-120. B FP of FITC-labeled mIGF2 with varying concentrations of BiP (red), Grp94 (blue), and BiP and Grp94 (green) under ADP conditions. C Change in FP (ΔP) of FITC-labeled proIGF225-120 with 5 μM BiP, 5 μM Grp94 monomer, and ADP, in the presence and absence of inhibitors, and various BiP and Grp94 mutants. D. Schematic of inhibitor structural effects on ternary complex formation of BiP, Grp94, and proIGF2 client. Error bars are SEM for three independent replicate measurements. Source data are provided as a Source Data file.
