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3T98

Molecular Architecture of the Transport Channel of the Nuclear Pore Complex: Nup54/Nup58

Summary for 3T98
Entry DOI10.2210/pdb3t98/pdb
Related2OSZ 3T97
DescriptorNuclear pore complex protein Nup54, Nucleoporin Nup58/Nup45 (3 entities in total)
Functional Keywordsnup58, nup54, nup62 complex, nuclear import, coiled-coil, helix, hairpin, fg-repeat, nucleoporin, npc, nuclear tranport, transport channel, nup62, nup45, nup93, karyopherin, nuclear pore complex, nuclear pore domain, nuclear envelope, protein transport
Biological sourceRattus norvegicus (rat)
More
Cellular locationNucleus, nuclear pore complex: P70582 P70581
Total number of polymer chains3
Total formula weight22788.94
Authors
Solmaz, S.R.,Blobel, G.,Melcak, I. (deposition date: 2011-08-02, release date: 2011-11-02, Last modification date: 2024-02-28)
Primary citationSolmaz, S.R.,Chauhan, R.,Blobel, G.,Melcak, I.
Molecular architecture of the transport channel of the nuclear pore complex.
Cell(Cambridge,Mass.), 147:590-602, 2011
Cited by
PubMed Abstract: The nuclear pore complex encloses a central channel for nucleocytoplasmic transport, which is thought to consist of three nucleoporins, Nup54, Nup58, and Nup62. However, the structure and composition of the channel are elusive. We determined the crystal structures of the interacting domains between these nucleoporins and pieced together the molecular architecture of the mammalian transport channel. Located in the channel midplane is a flexible Nup54⋅Nup58 ring that can undergo large rearrangements yielding diameter changes from ∼20 to ∼40 nm. Nup62⋅Nup54 triple helices project alternately up and down from either side of the midplane ring and form nucleoplasmic and cytoplasmic entries. The channel consists of as many as 224 copies of the three nucleoporins, amounting to a molar mass of 12.3 MDa and contributing 256 phenylalanine-glycine repeat regions. We propose that the occupancy of these repeat regions with transport receptors modulates ring diameter and transport activity.
PubMed: 22036567
DOI: 10.1016/j.cell.2011.09.034
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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