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Science 23 March 2007:
Vol. 315. no. 5819, pp. 1729 - 1732
DOI: 10.1126/science.1135730
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Reports

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

Ivo Melcák, André Hoelz,* Günter Blobel*

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 {alpha}-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.

Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.

* To whom correspondence should be addressed. E-mail: hoelza{at}rockefeller.edu (A.H.), blobel{at}rockefeller.edu (G.B.)

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Science. ISSN 0036-8075 (print), 1095-9203 (online)