Structure of Nup58/45 Suggests Flexible Nuclear Pore Diameter by Intermolecular Sliding
2007; American Association for the Advancement of Science; Volume: 315; Issue: 5819 Linguagem: Inglês
10.1126/science.1135730
ISSN1095-9203
AutoresIvo Melčák, André Hoelz, Günter Blobel,
Tópico(s)Genomics and Chromatin Dynamics
ResumoThe 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.
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