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Switching affinities in nuclear trafficking

Nature Structural Biology volume 6, pages 301–304 (1999)Cite this article

Abstract

A new structure of full length importin α, a key protein in the nuclear transport process, lends support to a model of autoinhibition mediated by importin α residues that mimic a nuclear localization sequence. This model explains the change in importin α affinity for nuclear localization sequences that occurs in transporting cargo from the cytoplasm to the nucleus.

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Figure 1: Schematic illustration of the molecular components of the nuclear protein import machinery.
Figure 3: Cα trace of mouse importin α showing the IBB domain in CPK representation8.
Figure 2: Structure of the Arm (armadillo) and HEAT repeats from which importins α and β are constructed.
Figure 4: Stereo views of the interaction between a, SV40 NLS and yeast importin α4 (PDB code 1bk6) and between b, mouse importin α and its IBB domain8 (PDB code 1ia1).

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  1. the MRC Laboratory of Molecular Biology, Hills Rd., Cambridge, CB2 2QH, UK

    Murray Stewart & Daniela Rhodes

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  2. Daniela Rhodes
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Correspondence to Murray Stewart or Daniela Rhodes.

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Stewart, M., Rhodes, D. Switching affinities in nuclear trafficking. Nat Struct Mol Biol 6, 301–304 (1999). https://doi.org/10.1038/7529

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