Extended Data Fig. 5: Isoforms and Noonan Syndrome mutations of PP1C.
From: Structure of the SHOC2–MRAS–PP1C complex provides insights into RAF activation and Noonan syndrome
a Sequence alignment of the three human isoforms of PP1C. Totally conserved residues are bold and highlighted in black, while similar residues are bold and highlighted in white. Non-conserved residues are only highlighted in white. The secondary structure of the PP1CA structure is shown above the alignment. α-helices and β-strands are labeled according to the nomenclature of Peti et al.29. Residues of PP1CA which interact with SHOC2 and MRAS are denoted with pink ovals and blue stars, respectively. R188 is the only residue of PP1CA which interacts with both SHOC2 and MRAS. b Single-cycle kinetic analysis was performed on immobilized avi-tagged SHOC2 with five injections of MRASGMPPNP and PP1CA mutants as denoted in the figure (blue). The data were fit to a 1:1 kinetic model (black).
