2osz | pdb_00002osz
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Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding
Overview
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.
About this Structure
2OSZ is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding., Melcak I, Hoelz A, Blobel G, Science. 2007 Mar 23;315(5819):1729-32. PMID:17379812
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