2osz: Difference between revisions

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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.

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==

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[[Category: structure]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 20: / Line 20: @@
 [[Category: structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:25:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:22:13 2008''