Figure 9
From: Discovery of Small Molecules that Inhibit the Disordered Protein, p27Kip1
Distance profiles of W60, W76 and Y88 Cβ atoms monitored as a function of time from MD simulations reveal extended and compact states in the p27-D2 conformational ensemble.
(a) Distance between W60-W76 (left), W60-Y88 (center) and W76-Y88 (right) Cβ atoms monitored over time from MD with gray lines representing the instantaneous distance (every 2 ps) and red lines representing the time average (every one ns). The times at which representative extended (E) and compact (C) conformers were extracted for display in Suppl. Fig. 10 are indicated. (b) Illustration of the distributions of the distances in (a) shown as histograms (red lines). The distributions show the existence of two distinct states for W60-Y88 (center) and W76-Y88 (right) indicating compact (C) and extended (E) conformations (see Suppl. Fig. 10). (c,d) Representative extended (c) and compact (d) conformations, respectively, showing relative positions of residues of p27-D2 involved in interaction with fragment hits.
