Binding dynamics of isolated nucleoporin repeat regions to importin-beta

Structure. 2005 Dec;13(12):1869-79. doi: 10.1016/j.str.2005.09.007.


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-beta 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-beta 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-beta may be necessary for the pore complex to distinguish between importin-beta and inert proteins, and to allow for its passage through the pore.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Computer Simulation
  • Conserved Sequence
  • Crystallography, X-Ray
  • Glycine / chemistry
  • Mice
  • Molecular Sequence Data
  • Nuclear Pore Complex Proteins / chemistry*
  • Phenylalanine / chemistry
  • Protein Conformation
  • Repetitive Sequences, Amino Acid*
  • beta Karyopherins / chemistry*


  • Nuclear Pore Complex Proteins
  • beta Karyopherins
  • Phenylalanine
  • Glycine