Structure and gating of the nuclear pore complex

Nat Commun. 2015 Jun 26:6:7532. doi: 10.1038/ncomms8532.


Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we analyse the structure of the NPC scaffold and permeability barrier, by reconstructing the Xenopus laevis oocyte NPC from native nuclear envelopes up to 20 Å resolution by cryo-electron tomography in conjunction with subtomogram averaging. In addition to resolving individual protein domains of the NPC constituents, we propose a model for the architecture of the molecular gate at its central channel. Furthermore, we compare and contrast this native NPC structure to one that exhibits reduced transport activity and unveil the spatial properties of the NPC gate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cryoelectron Microscopy
  • Humans
  • Imaging, Three-Dimensional / methods*
  • Ion Channel Gating / physiology*
  • Models, Molecular
  • Multiprotein Complexes / chemistry
  • Multiprotein Complexes / ultrastructure
  • Nuclear Pore / chemistry*
  • Nuclear Pore / ultrastructure*
  • Oocytes / ultrastructure*
  • Protein Conformation
  • Xenopus laevis


  • Multiprotein Complexes