4.8 Article

Architecture of the nuclear pore complex coat

Journal

SCIENCE
Volume 347, Issue 6226, Pages 1148-1152

Publisher

AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaa4136

Keywords

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Funding

  1. Gordon and Betty Moore Foundation
  2. Beckman Institute
  3. Sanofi-Aventis Bioengineering Research Program
  4. U.S. Department of Energy
  5. National Institues of Health (NIH)
  6. National Cancer Institute [ACB-12002]
  7. National Institute of General Medical Sciences [AGM-12006]
  8. Postdoctoral Fellowship of the Deutsche Forschungsgemeinschaft
  9. NIH Research Service Award [5 T32 GM07616]
  10. NIH [U01 GM094588, U54 GM087519]
  11. Searle Funds at The Chicago Community Trust
  12. Caltech startup funds
  13. Albert Wyrick V Scholar Award of the V Foundation for Cancer Research
  14. 54th Mallinckrodt Scholar Award of the Edward Mallinckrodt Jr. Foundation
  15. Kimmel Scholar Award of the Sidney Kimmel Foundation for Cancer Research

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The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. Despite half a century of structural characterization, the architecture of the NPC remains unknown. Here we present the crystal structure of a reconstituted similar to 400-kilodalton coat nucleoporin complex (CNC) from Saccharomyces cerevisiae at a 7.4 angstrom resolution. The crystal structure revealed a curved Y-shaped architecture and the molecular details of the coat nucleoporin interactions forming the central triskelion of the Y. A structural comparison of the yeast CNC with an electron microscopy reconstruction of its human counterpart suggested the evolutionary conservation of the elucidated architecture. Moreover, 32 copies of the CNC crystal structure docked readily into a cryoelectron tomographic reconstruction of the fully assembled human NPC, thereby accounting for similar to 16 megadalton of its mass.

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