Fig. 1
From: Computational insights into the allosteric behavior of mini proinsulin driven by C peptide mobility
Structural representation of mini-analogs for calculated and experimental co-complexes. (A) AlphaFold prediction of the novel designer mini-proinsulin (nMPI2). (B) Experimental structure of mini-proinsulin from the Protein Data Bank (PDB ID: 1EFE), referred to as MPI2. (C) Experimental structure of native insulin from the PDB (ID: 3I40). RMSD values between the structures are indicated with bidirectional arrows. (D) Docking co-complex of the experimental insulin receptor (IR, shown in green) and nMPI2, indicating a relatively higher affinity score. (E) Docking co-complex of the experimental IR (green) and MPI2, indicating a relatively lower affinity score. (F) Experimental IR-INS Cryo-EM co-complex from the PDB (ID: 6VEP). (G–I) Poisson-Boltzmann electrostatics of the docking and experimental co-complexes, illustrating the charge-smoothed protein contact potential. Red regions represent areas of negative electrostatic potential, blue regions indicate areas of positive electrostatic potential, and white (or neutral) regions represent areas with near-neutral electrostatic potential.
