Science Advances

Supplementary Materials

This PDF file includes:

  • Fig. S1. Characterization of the N- and C-terminal regions of Nup53 and their interactions with Nic96, Nup157, and Kap121.
  • Fig. S2. Kap121 interacts with the C-terminal region of Nup53 using the NLS and FG motif binding sites.
  • Fig. S3. The RRM domain of human Nup53 forms a constitutive dimer in solution.
  • Fig. S4. The RRM domain enhances biphasic profile of 53core-Kap121 interactions.
  • Fig. S5. NS-EM analysis of Nup53-Kap121 interactions.
  • Fig. S6. Reconstitution of Nup53 into complexes with Nic96 and Nup157.
  • Fig. S7. Kap121 allosterically destabilizes Nic96 interactions with dimerization-deficient Nup53.
  • Fig. S8. NS-EM analysis of the Kap121·53core·Nic96 complex.
  • Table S1. Bacterial expression constructs.
  • Table S2. Data collection and refinement statistics for the ScNup53 RRM domain (molecular replacement).
  • References (5861)

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