A Jumbo Problem: Mapping the Structure and Functions of the Nuclear Pore Complex

Curr Opin Cell Biol. 2012 Feb;24(1):92-9. doi: 10.1016/j.ceb.2011.12.013. Epub 2012 Feb 8.


Macromolecular assemblies can be intrinsically refractive to classical structural analysis, due to their size, complexity, plasticity and dynamic nature. One such assembly is the nuclear pore complex (NPC). The NPC is formed from ∼450 copies of 30 different proteins, called nucleoporins, and is the sole mediator of exchange between the nucleus and the cytoplasm in eukaryotic cells. Despite significant progress, it has become increasingly clear that new approaches, integrating different sources of structural and functional data, will be needed to understand the functional biology of the NPC. Here, we discuss the latest approaches trying to address this challenge.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Cell Nucleus / metabolism
  • Cytoplasm / metabolism
  • Eukaryotic Cells / cytology
  • Eukaryotic Cells / metabolism*
  • Humans
  • Molecular Structure
  • Nuclear Pore / chemistry*
  • Nuclear Pore / metabolism*
  • Nuclear Pore Complex Proteins / chemistry
  • Nuclear Pore Complex Proteins / metabolism*
  • Structure-Activity Relationship


  • Nuclear Pore Complex Proteins