Extended Data Fig. 5: Detailed interactions between FEM1C and C-degrons.
From: Molecular basis for arginine C-terminal degron recognition by Cul2FEM1 E3 ligase
a, The electrostatic surface of the FEM1C ankyrin repeats (1-240) bound with OR51B2, with the peptides shown in yellow sticks and labelled. b, Recognition of −4RFSR−1 (R-X-X-R) by FEM1C. The peptide residues and FEM1C residues involved in the intermolecular interactions are labelled, and shown in yellow and blue sticks, respectively. c, The electrostatic surface of the FEM1C ankyrin repeats (1-240) bound with the Clone13 −6TQGRAR−1, d, Recognition of −4GRAR−1 (R-X-R) by FEM1C. e, The electrostatic surface of the FEM1C ankyrin repeats (1-240) bound with the peptide −7LLKELRG−1. f, Recognition of −5KELRG−1 (K-X-X-RG) by FEM1C. g, The electrostatic surface of the FEM1C ankyrin repeats (1-240) bound with CDK5R1. (h) Recognition of −9KRLLLGLDR−1 by FEM1C. (c), (e), and (g) are shown in a manner similar to that shown in Extended Data Fig. 5a, while (d), (f), and (h) are shown in a way similar to that shown in Extended Data Fig. 5b.
