Fig. 1: An overview of sequence and structural characteristics of eIF4B.
From: Disordered regions of human eIF4B orchestrate a dynamic self-association landscape
a Cartoon representation of human eIF4B based on the RRM domain structure (PDB: 2J76) and predicted IDR structural propensity from AlphaFold2. b Schematic domain representation of human eIF4B, together with a disorder prediction plot based on IUPred391 (dark blue) and the prediction of polyproline II secondary structure propensity (gray)92. The structured RRM domain and short disordered N-terminal tail are shadowed in gray. The boundaries of protein constructs used in this work are also indicated. c Amino acid distribution plots for negative (D and E, shown in red and purple, respectively), positive (R and K, shown in teal and light blue, respectively), aromatic (Y, F and W, shown in orange, brown and yellow, respectively), glycine (G, shown in black) and proline (P, shown in green) residues, particularly highlighting clustering of these residues within several subregions, i.e. DRYG-rich region (residues 214–327; highlighted in light orange), RE-rich region (residues 367–455; highlighted in light blue) and the P-rich region (residues 460–522; highlighted in light green). Source data are provided as a Source Data file.
