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PDBsum entry 3f7f
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Structural protein
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PDB id
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3f7f
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References listed in PDB file
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Key reference
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Title
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Structural and functional analysis of nup120 suggests ring formation of the nup84 complex.
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Authors
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H.S.Seo,
Y.Ma,
E.W.Debler,
D.Wacker,
S.Kutik,
G.Blobel,
A.Hoelz.
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Ref.
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Proc Natl Acad Sci U S A, 2009,
106,
14281-14286.
[DOI no: ]
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PubMed id
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Abstract
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The Nup84 complex constitutes a key building block in the nuclear pore complex
(NPC). Here we present the crystal structure of one of its 7 components, Nup120,
which reveals a beta propeller and an alpha-helical domain representing a novel
fold. We discovered a previously unidentified interaction of Nup120 with Nup133
and confirmed the physiological relevance in vivo. As mapping of the individual
components in the Nup84 complex places Nup120 and Nup133 at opposite ends of the
heptamer, our findings indicate a head-to-tail arrangement of elongated Nup84
complexes into a ring structure, consistent with a fence-like coat for the
nuclear pore membrane. The attachment site for Nup133 lies at the very end of an
extended unstructured region, which allows for flexibility in the diameter of
the Nup84 complex ring. These results illuminate important roles of terminal
unstructured segments in nucleoporins for the architecture, function, and
assembly of the NPC.
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Figure 2.
Structural analysis of the Nup120 NTD domains. (A) Ribbon
representation of the Nup120 β propeller domain. The 7 blades
of the β propeller core (yellow), the location of the
disordered 1E1A loop (orange), the 3D4A loop (red), the
α-helical insertion in the 6D7A loop (blue), and their
secondary structure elements are indicated. (B) Schematic
representation of the Nup120 β propeller domain and the
locations of its various insertions. (C) Ribbon representation
of the Nup120 α-helical domain. The leucine zipper–like core
(orange) and the 9 surrounding α-helices (green) are indicated.
A 180°-rotated view is shown on the right.
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Figure 5.
Model for the ring formation of the Nup84 complex. (A)
Schematic representation of the heptameric complex and the
approximate localization of its 7 nups (19). (B) The interaction
of Nup120 and Nup133 suggests the intermolecular interaction
between 2 heptamers in a head-to-tail fashion mediated by a
short stretch at the very N terminus of an extended unstructured
region of Nup133. (C) Eight heptamers are arranged in a closed
ring with a diameter of ≈1,000 Å in accordance with the
NPC dimensions determined by cryo-electron microscopy (8).
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