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

A jumbo problem: mapping the structure and functions of the nuclear pore complex.

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1
Laboratory of Cellular and Structural Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.

Abstract

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.

PMID:
22321828
PMCID:
PMC3472030
DOI:
10.1016/j.ceb.2011.12.013
[Indexed for MEDLINE]
Free PMC Article

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