The Importin β Binding Domain Modulates the Avidity of Importin β for the Nuclear Pore Complex*

@article{Lott2010TheI,
  title={The Importin $\beta$ Binding Domain Modulates the Avidity of Importin $\beta$ for the Nuclear Pore Complex*},
  author={Kaylen Lott and Anshul Bhardwaj and Gregory Mitrousis and Nelly Pant{\'e} and Gino Cingolani},
  journal={The Journal of Biological Chemistry},
  year={2010},
  volume={285},
  pages={13769 - 13780}
}
Importin β mediates active passage of cellular substrates through the nuclear pore complex (NPC). Adaptors such as importin α and snurportin associate with importin β via an importin β binding (IBB) domain. The intrinsic structural flexibility of importin β allows its concerted interactions with IBB domains, phenylalanine-glycine nucleoporins, and the GTPase Ran during transport. In this paper, we provide evidence that the nature of the IBB domain modulates the affinity of the import complex… 

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