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PDBsum entry 1ibr
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Cell cycle,translation
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PDB id
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1ibr
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Contents |
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* Residue conservation analysis
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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 view of the ran-Importin beta interaction at 2.3 a resolution.
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Authors
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I.R.Vetter,
A.Arndt,
U.Kutay,
D.Görlich,
A.Wittinghofer.
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Ref.
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Cell, 1999,
97,
635-646.
[DOI no: ]
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PubMed id
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Abstract
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Transport receptors of the Importin beta family shuttle between the nucleus and
cytoplasm and mediate transport of macromolecules through nuclear pore
complexes. They interact specifically with the GTP-binding protein Ran, which in
turn regulates their interaction with cargo. Here, we report the
three-dimensional structure of a complex between Ran bound to the
nonhydrolyzable GTP analog GppNHp and a 462-residue fragment from Importin beta.
The structure of Importin beta shows 10 tandem repeats resembling HEAT and
Armadillo motifs. They form an irregular crescent, the concave site of which
forms the interface with Ran-triphosphate. The importin-binding site of Ran does
not overlap with that of the Ran-binding domain of RanBP2.
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Figure 4.
Figure 4. Structure of the Complex(A) Schematic
representation of the structure of the complex, indicating the
contacts of residues on Impβ with those of Ran. Interactions
found in only one of the two molecules have an additional A,B
identifier on the residue number. Open circles in Impβ[N]
indicate the position of the B helices of the repeats with their
numbers in red.(B) Ribbon representation of the complex with Ran
in red, Impβ in green, superimposed with RanGDP in blue to
highlight the potential clashes in switch I and the C-terminal
end. GppNHp and Mg^2+ are shown as black ball-and-stick
models.(C) Electrostatic surface potential of Impβ and
RanGppNHp in and close to the interface (GRASP; [53]). The
180° rotation of Ran is indicated.
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Figure 5.
Figure 5. Flexibility of ImpβB factor representation of the
two Impβ molecules in the asymmetric unit of the crystal with a
color code, where red indicates high B factors and blue
indicates low B factors. This indicates the different
flexibilities in the two molecules, both inside and outside the
Ran interface.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1999,
97,
635-646)
copyright 1999.
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Secondary reference #1
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Title
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Identification of different roles for rangdp and rangtp in nuclear protein import.
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Authors
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D.Görlich,
N.Panté,
U.Kutay,
U.Aebi,
F.R.Bischoff.
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Ref.
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Embo J, 1996,
15,
5584-5594.
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PubMed id
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Secondary reference #2
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Title
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Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope.
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Authors
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D.Görlich,
S.Kostka,
R.Kraft,
C.Dingwall,
R.A.Laskey,
E.Hartmann,
S.Prehn.
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Ref.
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Curr Biol, 1995,
5,
383-392.
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PubMed id
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Secondary reference #3
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Title
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Sequence and characterization of cytoplasmic nuclear protein import factor p97.
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Authors
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N.C.Chi,
E.J.Adam,
S.A.Adam.
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Ref.
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J Cell Biol, 1995,
130,
265-274.
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PubMed id
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