Structure of Nup58/45 Suggests Flexible Nuclear Pore Diameter by Intermolecular Sliding
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.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 930662
- Report Number(s):
- BNL-81155-2008-JA; SCEHDK; TRN: US200901%%168
- Journal Information:
- Science, Vol. 315; ISSN 0193-4511
- Country of Publication:
- United States
- Language:
- English
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