Fig. 3: Biochemical–physical and structural evidence of SHOC2 in complex with oncogenic canonical RAS proteins.
From: Targeting the SHOC2–RAS interaction in RAS-mutant cancers
a, Sedimentation velocity profiles expressed as c/s distribution plots. Monomeric sedimentation coefficients (S) were observed for SHOC2 (blue) and NRAS (grey), while NRAS(Q61R)–GTP mixed with SHOC2 (orange) displayed larger S values consistent with a binary complex. A representative example of three independent experiments is shown. b, Surface and ribbon representation of the binary interaction of SHOC2 (light violet) and NRAS(Q61R) (grey) (Protein Data Bank: 9BTM). RAS-bound magnesium is shown as a green sphere adjacent to the stick representation of GTP. c, The interaction between SHOC2 and MRAS(Q71R) (orange; SMP complex structure with PP1Cα hidden) or NRAS(Q61R) (grey) is shown aligned through the SHOC2 solenoid (light violet; model shown from the SHOC2–NRAS binary structure), highlighting the difference in orientation between the binary and ternary complex models when aligned with the SHOC2 solenoid as the key object. d, Detailed representation of key interactions between NRAS(Q61R) SWI (pink)/SWII (green) and SHOC2 (light violet).
