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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