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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5819
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pubmed:dateCreated |
2007-3-23
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
23
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pubmed:volume |
315
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1729-32
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:17379812-Amino Acid Sequence,
pubmed-meshheading:17379812-Animals,
pubmed-meshheading:17379812-Crystallization,
pubmed-meshheading:17379812-Crystallography, X-Ray,
pubmed-meshheading:17379812-Dimerization,
pubmed-meshheading:17379812-Hydrogen Bonding,
pubmed-meshheading:17379812-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:17379812-Membrane Glycoproteins,
pubmed-meshheading:17379812-Molecular Sequence Data,
pubmed-meshheading:17379812-Nuclear Pore Complex Proteins,
pubmed-meshheading:17379812-Protein Folding,
pubmed-meshheading:17379812-Protein Structure, Quaternary,
pubmed-meshheading:17379812-Protein Structure, Secondary,
pubmed-meshheading:17379812-Protein Structure, Tertiary,
pubmed-meshheading:17379812-Protein Subunits,
pubmed-meshheading:17379812-Rats,
pubmed-meshheading:17379812-Static Electricity
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pubmed:year |
2007
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pubmed:articleTitle |
Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding.
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pubmed:affiliation |
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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