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PDBsum entry 4kf7
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Structural protein
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PDB id
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4kf7
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References listed in PDB file
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Key reference
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Title
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Scaffold nucleoporins nup188 and nup192 share structural and functional properties with nuclear transport receptors.
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Authors
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K.R.Andersen,
E.Onischenko,
J.H.Tang,
P.Kumar,
J.Z.Chen,
A.Ulrich,
J.T.Liphardt,
K.Weis,
T.U.Schwartz.
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Ref.
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Elife, 2013,
2,
e00745.
[DOI no: ]
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PubMed id
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Abstract
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Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs)
embedded in the nuclear envelope. About 30 different proteins (nucleoporins,
nups) arrange around a central eightfold rotational axis to build the modular
NPC. Nup188 and Nup192 are related and evolutionary conserved, large
nucleoporins that are part of the NPC scaffold. Here we determine the structure
of Nup188. The protein folds into an extended stack of helices where an
N-terminal 130 kDa segment forms an intricate closed ring, while the C-terminal
region is a more regular, superhelical structure. Overall, the structure has
distant similarity with flexible S-shaped nuclear transport receptors (NTRs).
Intriguingly, like NTRs, both Nup188 and Nup192 specifically bind FG-repeats and
are able to translocate through NPCs by facilitated diffusion. This blurs the
existing dogma of a clear distinction between stationary nups and soluble NTRs
and suggests an evolutionary relationship between the NPC and the soluble
nuclear transport machinery. DOI:http://dx.doi.org/10.7554/eLife.00745.001.
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