Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking.

By R. Bayliss, T. Littlewood, M. Stewart. 2000

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The Importin β Binding Domain as a Master Regulator of Nucleocytoplasmic Transport (2010, unknown): “The crystal structure of importin β bound to an FxFG fragment of a nucleoporin revealed that FG-repeats bind the convex surface of importin β, on the opposite surface as adaptor and Ran [33].”
Transport into and out of the Nucleus (2001, unknown): “Assuming a diffusion-limited on-rate ( 7 109 M 1 s 1 at 37°C) and a Kd for the interaction of a carrier with an FG repeat of about 25 M (based on the value for NTF2/Nsp1 binding), the dissociation constant would be about 2 105 s 1 (34).”
Comprehending crystalline β-carotene accumulation by comparing engineered cell models and the natural carotenoid-rich system of citrus (2011, unknown): “Bayliss et al. (2000) determined the crystal structure of the human transport receptor, importin β, and identified its two FG repeat binding sites.”
Mechanisms of Receptor‐Mediated Nuclear Import and Nuclear Export (2005, unknown): “Two hydrophobic pockets are formed in the karyopherin by the side chains of residues between HEAT repeats 5 and 6 and, 6 and 7, into which the phenylalanines of FG repeats are inserted (46).”
Smad transcription factors. (2005, background): “The FG repeat region is also the region for nucleoporin interaction with importins (Bayliss et al. 2000).”