Extended Data Fig. 9: Comparison of the Arg/C-degron recognition by FEM1C with that of Gly/C-degron by KLHDC2. The electrostatic surface of FEM1C and KHLDC2 are shown.
From: Molecular basis for arginine C-terminal degron recognition by Cul2FEM1 E3 ligase
a, SIL1 binding surface of FEM1C. The SIL1 peptide is shown in yellow ribbon, with Arg-1 and Lys-4 sown in sticks. FEM1C residues involved in the interaction with Arg-1 and Lys-4 are also shwon in sticks. b, di-glycine binding surface of KHLDC2 (PDB: 6DO3). The di-glycine are shown in yellow sticks, and the KLHDC2 residues involved in binding to di-glycine are also shown in sticks.
