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. 2018 Mar 19;46(7):3791–3801. doi: 10.1093/nar/gky194

Figure 2.

Figure 2.

Comparison of key interaction motifs between Leish(IF4E-1/4E-IP1) complex and human eIF4E/4E-BP1 or Drosophila eIF4E/Cup complexes. (A) Cartoon representation of the structural alignment of the Leish(IF4E-1/4E-IP11-52) and the mammalian eIF4E/m7GTP/4E-BP1 complex [PDB ID: 5BXV, (31)]. The Leish(IF4E-1/4E-IP11–52) complex is represented and colored as described in Figure 1. eIF4E and 4E-BP1 are shown in orange and yellow, respectively. The m7GTP cap in the eIF4E/4E-BP1 complex is omitted for clarity. (B) As described in (A) but showing key interactions centered on the consensus binding motifs [Y(X)4LΦ] of Leish4E-IP1. Key residues are indicated. (C) As described in (A) but showing interactions centered on the linker region of Leish4E-IP1 (See also Figure 1A–C). (D) As described in (A) but showing interactions over the C-terminal tail of Leish4E-IP1. (E) Structural alignment of Leish(IF4E-1/4E-IP11–52) and the eIF4E/Cup complex from Drosophila melanogaster [PDB ID: 4AXG, (46)]. eIF4E and Cup are shown in pink and green, respectively. The linker segment of Cup is disordered in the complex and is shown as dashed lines (See also Supplementary Figure S1B and S4).