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Published March 23, 2007 | Supplemental Material
Journal Article Open

Structure of Nup58/45 Suggests Flexible Nuclear Pore Diameter by Intermolecular Sliding


The nucleoporins Nup58 and Nup45 are part of the central transport channel of the nuclear pore complex, which is thought to have a flexible diameter. In the crystal structure of an α-helical region of mammalian Nup58/45, we identified distinct tetramers, each consisting of two antiparallel hairpin dimers. The intradimeric interface is hydrophobic, whereas dimer-dimer association occurs through large hydrophilic residues. These residues are laterally displaced in various tetramer conformations, which suggests an intermolecular sliding by 11 angstroms. We propose that circumferential sliding plays a role in adjusting the diameter of the central transport channel.

Additional Information

© 2007 American Association for the Advancement of Science. Received 29 September 2006; accepted 16 February 2007. We thank Š. Melčáková, M. Müller, and T. Schwartz for help at the initial stages of the project; L. Gerace for the gift of cDNAs; B. Manjasetty (National Synchrotron Light Source) and C. Ralston (Advanced Light Source) for their excellent scientific support and help with x-ray measurements; T. Huber for stimulating discussions; E. Coutavas, M. King, A. Patke, and S. Solmaz for critical reading of the manuscript; and S. Etherton for help with editing of the manuscript. A.H. was supported by a grant from the Leukemia and Lymphoma Society. G.B. is an investigator of the Howard Hughes Medical Institute. The coordinates and structure factors have been deposited in the Protein Data Bank (accession code 2OSZ).

Attached Files

Supplemental Material - 1135730smov1.mpg

Supplemental Material - 1135730smov2.mpg

Supplemental Material - 1135730smov3.mpg

Supplemental Material - Melcak_SOM.pdf


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