Figure 3
From: NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation
LPS-induced NLRP6 dimers assemble into higher molecular oligomers in the presence of ATP. (a) Elution profiles of NLRP6 monomer (blue), NLRP6 monomer incubated with ATP (green), NLRP6 dimer (incubated with LPS, orange) and NLRP6 oligomer (incubated with both LPS and ATP, red) in Superdex 200 size exclusion chromatography. Panel insert shows the SDS-PAGE of protein fractions in peak 1, 2 and 3. (b) The formation of NLRP6 oligomers is ATP concentration dependent. (c) Representative particles of various NLRP6 oligomers in Peak 3. (d) Comparison of representative experimentally determined class averages (below) to 2D reprojections of the reconstructed 3D volume (above) of NLRP6 tetramer. (e) 3D reconstruction of NLRP6 tetramer, as shown in three orientations. Two boat shaped dimer units link together in a head-to-head manner. (f) Model fitting of NLRP6 tetramer with the computational model of NLRP6 dimer. (g) A cartoon model showing a 120° anti-clock deflection between two dimer units. See also Supplementary Fig. 3, Supplementary Movie 1.
