2osz | pdb_00002osz
Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding
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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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