Extended Data Fig. 4. PP1C makes extended interactions with SHOC2 and the MRAS effector surface.

a. PP1Cα interacts with SHOC2 across an extended arc of residues that localize to the ascending loop of SHOC2 LRRs. These interactions are primarily hydrophilic and become more networked near the N-terminal SHOC2 LRRs. Selected residues with salt bridge and hydrogen bond interactions are labelled. b. Helix G of PP1 (purple) and SWI(pink)/Strand beta 2 (grey) are the primary interaction surfaces of the MRAS/PP1Cα PPI. Key interacting residues are labelled. c. PP1C sequence alignment. Amino acid sequences of human PP1Cα, PP1Cβ, and PP1Cγ are aligned with PP1C sequences from frog, fly and worm. Identically conserved residues are shaded in red. Secondary structure elements of PP1C are indicated above the alignment. Symbols above the alignment indicate residues that in the holoenzyme complex lie in the interface with SHOC2 (green dots) or MRAS (blue diamonds).