Concerted regulation of npc2 binding to endosomal/lysosomal membranes by bis(monoacylglycero)phosphate and sphingomyelin
Fig 3
The free energy surfaces for npc2 binding to membranes.
A) Potential of mean force (pmf) profiles shown as a function of min zr, which stands for the minimum of the protein Cα z-coordinates for the residue r. The origin (z = 0) is set to comz of the upper leaflet P atoms. B) pmf surfaces shown as a function of min zr and ϕ for anionic membranes. Contours were plotted every 2 kJ/mol increments. The two binding orientations are marked with dashed lines. The thumbnail images of npc2 structure for the corresponding orientations are shown on the upper left corner for Prone mode and on the upper right corner for Supine mode. See S9 Fig for the local errors and S1 Fig for the pmf projected onto |z|. The labels indicate membrane content in molar fractions for a mixture of bmp:chol:sm:dopg:popc, and the corresponding system numbers (Table 1) are provided in parentheses. The local errors are given in S9 Fig.