Figure 4.
Predicted docking poses for the NLS of NUPR1 on importin. (A) Backbone (–N–Cα–C– atoms) representation of the best eight docking poses on ΔImportin for the wt sequence ERKLVTKLQ (the N terminus is on the top), which constitutes the core region for the NLS of NUPR1. (B) Most favorable binding pose for the same sequence (cyan), compared to the crystallographic conformation [46] of the NLS of the Epstein-Barr virus EBNA-LP protein (purple). For clarity, atoms are shown in standard colors only in the side chains of the two peptides, and the main-chain O and H atoms are omitted; apolar H atoms are not present. (C) Trp residues (brown) in the major NLS-binding site of importin play a key role in the binding of the most favorable conformation of the NLS of wild-type NUPR1. The view is slightly rotated with respect to previous representations to evidence the tryptophan side chains. (D) Most favorable docking poses for the eight peptide sequences: wild type (cyan), K65A (magenta), K69A (yellow), T68E (blue), K65AT68E (red), T68EK69A (green), K65AT68EK69A (orange), and pT68 (violet). PyMol was used for all displays.