Structural highlights
Function
[NUPL1_RAT] Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hu T, Guan T, Gerace L. Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins. J Cell Biol. 1996 Aug;134(3):589-601. PMID:8707840
- ↑ Melcak I, Hoelz A, Blobel G. Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding. Science. 2007 Mar 23;315(5819):1729-32. PMID:17379812 doi:315/5819/1729
