Extended Data Fig. 3: Identification of BRISC dimers in mass photometry and native mass spectrometry.
From: Molecular glues that inhibit deubiquitylase activity and inflammatory signaling
a, Native mass spectra of BRISC mixed with DMSO (control), JMS-175-2, or FX-171-C. BRISC complexes and subcomplexes are highlighted. b, Table of calculated masses for different BRISC subcomplexes and super complexes. c, Mass photometry measurements of BRISC dimer at increasing inhibitor concentrations. Counts corresponding to BRISC dimer as a fraction of total counts are plotted. Data points are mean ± SEM from three independent experiments. d, Left, K63-linked diUb (dark grey) modelled on the MPN+ domain of BRCC36 in BRISC (light grey), based on the AMSH LP-diUb structure (PDB: 2ZNV). Right, Upon dimer formation, the second BRISC monomer sterically clashes with the proximal ubiquitin when it is bound to either BRCC36 active site.
