Fig. 1: SHOC2, PP1C and MRAS form a three-way complex in a GTP-dependent manner.
From: Structural basis for SHOC2 modulation of RAS signalling
a, SEC traces showing three-way SHOC2–PP1C–MRAS complex formation in the presence of MRAS(GCP) but not in the presence of MRAS(GDP) (top), with SDS–PAGE analysis of SEC fractions (bottom). Results are representative of two independent experiments. b, Cryo-EM density map of SHOC2 (green) PP1C (purple) MRAS (salmon) complex, unsharpened. c, Structure of the SHOC2–PP1C–MRAS complex showing GCP (yellow) and the PP1C active site exposed to solvent for substrate binding. d, Model of the SHOC2–PP1C–RAS complex anchored to the membrane via the prenylated C terminus of RAS (salmon shows MRAS(GCP) modelled with the C-terminal helix of farnesylated KRAS; Protein Data Bank (PDB) ID: 5TAR).
