Journal
SCIENCE
Volume 352, Issue 6283, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaf1015
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Funding
- U. S. Department of Energy
- National Institutes of Health (NIH)
- National Cancer Institute [ACB-12002]
- National Institute of General Medical Sciences [AGM-12006]
- NIH [5 T32 GM07616, R01-GM111461]
- Amgen Graduate Fellowship through the Caltech-Amgen Research Collaboration
- Deutsche Forschungsgemeinschaft
- Boehringer Ingelheim Fonds
- China Scholarship Council
- Caltech startup funds
- Albert Wyrick V Scholar Award from the V Foundation for Cancer Research
- 54th Mallinckrodt Scholar Award from the Edward Mallinckrodt Jr. Foundation
- Kimmel Scholar Award from the Sidney Kimmel Foundation for Cancer Research
- Camille-Dreyfus Teacher Scholar Award
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The nuclear pore complex (NPC) controls the transport of macromolecules between the nucleus and cytoplasm, but its molecular architecture has thus far remained poorly defined. We biochemically reconstituted NPC core protomers and elucidated the underlying protein-protein interaction network. Flexible linker sequences, rather than interactions between the structured core scaffold nucleoporins, mediate the assembly of the inner ring complex and its attachment to the NPC coat. X-ray crystallographic analysis of these scaffold nucleoporins revealed the molecular details of their interactions with the flexible linker sequences and enabled construction of full-length atomic structures. By docking these structures into the cryoelectron tomographic reconstruction of the intact human NPC and validating their placement with our nucleoporin interactome, we built a composite structure of the NPC symmetric core that contains similar to 320,000 residues and accounts for similar to 56 megadaltons of the NPC's structured mass. Our approach provides a paradigm for the structure determination of similarly complex macromolecular assemblies.
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