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PMID: 15837182 Published · ppublish English Journal Article Review

Modularity within the architecture of the nuclear pore complex.

Current opinion in structural biology ·Vol. 15 ·No. 2 ·2005-04-00 ·Pages 221-6

Schwartz TU

Abstract

Transport between nucleus and cytoplasm is exclusively mediated by nuclear pore complexes (NPCs) embedded in the nuclear envelope. The NPC is an enormously elaborate protein assembly, reflecting its ability to multitask by simultaneously regulating the trafficking of a diverse spectrum of substrates, ranging from microRNAs to assembled ribosomal subunits. The complexity and sheer size of the NPC have hampered efforts to elucidate its molecular architecture. However, recent studies using a battery of complementary techniques have significantly enhanced our understanding of the NPC structure. The picture of a highly dynamic and modular machine is emerging.

MeSH Terms
Binding Sites Computer Simulation Models, Chemical Models, Molecular Nuclear Envelope/chemistry Nuclear Pore/chemistry,ultrastructure Protein Binding Protein Conformation Protein Structure, Tertiary Structure-Activity Relationship
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Schwartz Thomas U
Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA. [email protected]
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
2005-04-00
Pages
221-6
Language
English
Region
England
NLM ID
9107784
Subset
IM
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