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. 2013 Feb 22;32(6):899–913. doi: 10.1038/emboj.2013.29

Figure 3.

Figure 3

Structural basis of Imp13 bidirectionality and KD affinities in the Imp13 cycle. (A) RanGTP and eIF1A concomitant interaction in the ternary export complex. Interacting residues on Ran and eIF1A are rendered as spheres in pink and sand, respectively. (B) Imp13-Mago-Y14 structure oriented as in Figure 3A (pdb ids.: 2x1g). Imp13 is represented as loop trace. A dashed line in black marks the boundary between compatible and hindered binding. (C) Protein co-precipitations by GST-tagged Imp13 incubated together with His-RanGTP and eIF1A with either wt or mutant proteins performed as in the previous figure. (D) Table representing KD values determined by DSF from at least three independent experiments.