Skip to main content
. 2012 Oct 19;7(10):e47235. doi: 10.1371/journal.pone.0047235

Figure 6. Comparison of 4EBP1 and eIF4G1 peptides suggests that eIF4E interacting peptides can form an ensemble of conformations when in complex with eIF4E.

Figure 6

A) An overlay of two eIF4E crystal structures complexed with either a 4EBP1 (1EJ4) or eIF4G1 (2W97) derived peptide demonstrating the deviation in their C-terminal structural conformations. 4EBP1 is shown in salmon and eIF4G1 in cyan. B) A plot of the φ and ψ angle distribution, derived from the 50 ns simulations of the peptides eIF4G1 and 4EBP bound to eIF4E, for the residues L10 and M10 respectively. C) A plot of the φ and ψ angle distributions, derived from the 50 ns simulations of peptides eIF4G1 and 4EBP bound to eIF4E, for the residues G11 and E11 respectively. D) A plot showing the distribution of distances, for the peptides eIF4G1 and 4E-BP1 when bound to eIF4E, between the Cα atoms of residues 6 and 10 versus the distance between the Cα atoms of residues 8 and 12. The distances were calculated from their respective 50 ns simulations for both peptides. E) A histogram of the angular distribution between the Cα atoms of positions 6, 8 and 10 of the eIF4G1 and 4EBP1 peptides from the 50ns simulations respectively.