Structural Basis for the Interaction between FxFG Nucleoporin Repeats and Importin-β in Nuclear Trafficking

@article{Bayliss2000StructuralBF,
  title={Structural Basis for the Interaction between FxFG Nucleoporin Repeats and Importin-$\beta$ in Nuclear Trafficking},
  author={Richard Bayliss and Trevor D. Littlewood and Murray Stewart},
  journal={Cell},
  year={2000},
  volume={102},
  pages={99-108}
}

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The crystal structure indicates that significant conformational changes occur when importin-β binds or releases the IBB domain domain and suggests how dissociation of the importIn-α/β heterodimer may be achieved upon nuclear entry.
Molecular interactions between the importin α/β heterodimer and proteins involved in vertebrate nuclear protein import
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The binding behaviour of p62 truncation mutants indicated that importin-β interacts primarily with the α-helical coiled-coil rod domain of nucleoporin p62 and not with the N-terminal domain that contains a number of degenerate repeats based on the xFxFG sequence motif.
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The 3.0 Å structure of the karyopherin-β2–Ran˙GppNHp complex is presented where Gpp NHp is a non-hydrolysable GTP analogue and provides a structural basis for the specificity of theKaryopherIn-β family for the GTP-bound state of Ran, as well as a rationale for interactions with the regulatory proteins ranGAP, ranGEF and ranBP1.
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TLDR
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TLDR
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