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. 2008 Oct 9;105(42):16101–16106. doi: 10.1073/pnas.0802647105

Fig. 5.

Fig. 5.

RanGTP-induced conformational change of FG-binding pockets. (A and B) The 3D structure of mouse importin-β was predicted from the crystal structure of yeast importin-β Kap95p (17, 20) complex with (red) and without (blue) RanGTP. The FG-binding site I (HEAT 5–7) (A) and the FG-binding site II (HEAT 14–16) (B) are shown. The amino acid side chains that have been expected to interact with the FG motifs (L174, T175, I178, E214, F217, M219, Q220, C223, Y255, P258, A259, A262, and I263 in site I, M608, A609, L612, Y646, A649, K651, P652, G655, F688, D690, E691, Q694 and L695 in site II) are shown (17, 21). (C) An illustration of the importin-β-Nup153 interaction and the effect of RanGTP. Upon binding of RanGTP to the amino-terminal domain, pocket Ia is inactivated via an allosteric effect, whereas pocket Ib is not affected. The binding of RanGTP also affects pocket IIb, but not IIa, through a far-reaching allosteric effect.