Binding dynamics of isolated nucleoporin repeat regions to importin-β

Timothy A. Isgro, Klaus Schulten

Research output: Contribution to journalArticlepeer-review

Abstract

The nuclear pore complex, through the interaction of its proteins with transport receptors, controls the transport of large molecules into and out of the cell's nucleus. There is ample evidence for proteins with FG sequence repeats playing an essential role in this control. Previous studies have elucidated binding spots for FG sequence repeats on the surface of the transport receptor importin-β by X-ray crystallography and mutational studies. Molecular dynamics simulations have been performed to characterize the interaction of FG sequence repeats with the transport receptor. Observed binding spots have been verified and novel sites discovered, suggesting that importin-β features many more binding spots than suspected so far. The observed binding spots are in accord with several models of nucleocytoplasmic transport, and the large number of binding spots on importin-β may be necessary for the pore complex to distinguish between importin-β and inert proteins, and to allow for its passage through the pore.

Original languageEnglish (US)
Pages (from-to)1869-1879
Number of pages11
JournalStructure
Volume13
Issue number12
DOIs
StatePublished - Dec 2005

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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