Fig. 1: I3 interaction with PP1.
From: Inhibitor-3 inhibits Protein Phosphatase 1 via a metal binding dynamic protein–protein interaction
A Domain structure of I3. PP1-specific SLiMs (SILK [teal], RVxF [turquoise] and CCC [dark pink]) are indicated. Additional constructs relevant to this figure are also shown. B SPR sensorgram for I31-126 and PP1α7-330. C SPR sensorgram for I31-126 RVxFdead and PP1α7-330. D 2D [1H,15N] HSQC spectrum of 15N-labeled I31-126 alone (black) and in complex with PP1α7-330 (red). E Peak intensity loss vs I3 protein sequence plot; SLIMs indicated with the same colors shown in A. F 2D [1H,15N] HSQC spectrum of 15N-labeled I31-126 RVxFdead alone (black) and in complex with PP1α7-330 (cyan). G SPR sensorgram for the minimal PP1 interaction domain of I3, I327-68, and PP1α7-330. H IC50 curves for PP1 inhibition by I31-126 and I327-68. IC50 values reported in Table 1. Data are presented as mean values ± SD, n = 4 technical replicates. I Crystal structure of the I327-68:PP1α7-300 complex with I3 shown as yellow sticks and PP1 shown as a surface; colors correspond to the binding pockets of the I3 motifs highlighted in the I3 sequence (below). I3 residues not modeled due to a lack of clear electron density indicated by dashed lines (also shown in italics in the sequence). J Plot of the I3 solvent accessible surface area buried per residue when I3 is bound to PP1.
