Fig. 7: The curvature of importin β is influenced by its binding partners. | Nature Communications

Fig. 7: The curvature of importin β is influenced by its binding partners.

From: Ran modulates allosteric crosstalk between importin β surfaces

Fig. 7: The curvature of importin β is influenced by its binding partners.

A An overlay of all the importin β structures solved by cryo-EM in this study, represented as beads-on-a-string. Among the importin β complexes, the xIBB-bound form adopts the longest solenoid, whereas the RanGTP-bound form is the shortest. Color coding: salmon, for importin β:xIBB; gray, for importin β:αIBB:FG; blue, for importin β:Ran-GTP; and orange, for importin β:Ran-GTP:RanBP1. B Rationalization of importin β domain movement based on DynDom analysis. Importin β consists of three clusters of HEAT repeats. Moving clusters I (HEATs 1–4) and III (HEATs 11–19) are depicted in blue, while the fixed cluster II (HEATs 5–10) is shown in gray. Bending helices H5B and H10B are shown in green.

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