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* Residue conservation analysis
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DOI no:
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Cell
97:635-646
(1999)
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PubMed id:
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Structural view of the Ran-Importin beta interaction at 2.3 A resolution.
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I.R.Vetter,
A.Arndt,
U.Kutay,
D.Görlich,
A.Wittinghofer.
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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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Selected figure(s)
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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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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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PDB codes:
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PDB codes:
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Genetics,
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Semin Cell Dev Biol,
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Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP.
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Science,
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PDB code:
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T.Zhang,
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Structure,
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PDB codes:
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A.May,
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Energy minimization in low-frequency normal modes to efficiently allow for global flexibility during systematic protein-protein docking.
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Proteins,
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Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure.
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EMBO J,
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PDB code:
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G.Mitrousis,
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PDB codes:
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PDB codes:
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N.Schrader,
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PDB code:
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Analysis of the signals and mechanisms mediating nuclear trafficking of GATA-4. Loss of DNA binding is associated with localization in intranuclear speckles.
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Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf.
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Structure,
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1618-1629.
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PDB codes:
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M.M.Higa,
S.L.Alam,
W.I.Sundquist,
and
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Molecular characterization of the Ran-binding zinc finger domain of Nup153.
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J Biol Chem,
282,
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PDB code:
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M.Stewart
(2007).
Molecular mechanism of the nuclear protein import cycle.
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Nat Rev Mol Cell Biol,
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Distant N- and C-terminal domains are required for intrinsic kinase activity of SMG-1, a critical component of nonsense-mediated mRNA decay.
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A.S.Madrid,
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Nuclear transport is becoming crystal clear.
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Chromosoma,
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98.
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B.J.Lee,
A.E.Cansizoglu,
K.E.Süel,
T.H.Louis,
Z.Zhang,
and
Y.M.Chook
(2006).
Rules for nuclear localization sequence recognition by karyopherin beta 2.
|
| |
Cell,
126,
543-558.
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PDB code:
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|
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E.Conti,
C.W.Müller,
and
M.Stewart
(2006).
Karyopherin flexibility in nucleocytoplasmic transport.
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Curr Opin Struct Biol,
16,
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H.Stark,
and
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(2006).
Cryo-electron microscopy of spliceosomal components.
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Annu Rev Biophys Biomol Struct,
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H.Yagisawa
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Nucleocytoplasmic shuttling of phospholipase C-delta1: a link to Ca2+.
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J Cell Biochem,
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D.Wohlwend,
and
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Transportin is a major nuclear import receptor for c-Fos: a novel mode of cargo interaction.
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J Biol Chem,
281,
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A.Hutton,
A.Yee,
C.H.Arrowsmith,
and
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(2006).
MTH187 from Methanobacterium thermoautotrophicum has three HEAT-like repeats.
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J Biomol NMR,
35,
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PDB code:
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R.Truant,
R.Atwal,
and
A.Burtnik
(2006).
Hypothesis: Huntingtin may function in membrane association and vesicular trafficking.
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Biochem Cell Biol,
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Crystallization and preliminary X-ray crystallographic studies of transportin 1 in complex with nucleocytoplasmic shuttling and nuclear localization fragments.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
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M.W.Kirschner,
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Domain structure of separase and its binding to securin as determined by EM.
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Nat Struct Mol Biol,
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Mechanisms of receptor-mediated nuclear import and nuclear export.
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Traffic,
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G.Mitrousis,
N.Walker-Kopp,
P.J.Sims,
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Phospholipid scramblase 1 contains a nonclassical nuclear localization signal with unique binding site in importin alpha.
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J Biol Chem,
280,
10599-10606.
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PDB code:
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M.M.Golas,
B.Sander,
C.L.Will,
R.Lührmann,
and
H.Stark
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Major conformational change in the complex SF3b upon integration into the spliceosomal U11/U12 di-snRNP as revealed by electron cryomicroscopy.
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Mol Cell,
17,
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M.Schmidt,
W.Haas,
B.Crosas,
P.G.Santamaria,
S.P.Gygi,
T.Walz,
and
D.Finley
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The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle.
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Nat Struct Mol Biol,
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Proteins,
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R.Kapon,
P.Hinterdorfer,
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Structural basis for nuclear import complex dissociation by RanGTP.
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Nature,
435,
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PDB code:
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T.A.Isgro,
and
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Binding dynamics of isolated nucleoporin repeat regions to importin-beta.
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Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling.
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PDB codes:
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A.Harel,
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Importin beta: conducting a much larger cellular symphony.
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Protein Sci,
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Crystal structure of MO25 alpha in complex with the C terminus of the pseudo kinase STE20-related adaptor.
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Nat Struct Mol Biol,
11,
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PDB codes:
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C.Petosa,
G.Schoehn,
P.Askjaer,
U.Bauer,
M.Moulin,
U.Steuerwald,
M.Soler-López,
F.Baudin,
I.W.Mattaj,
and
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(2004).
Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.
|
| |
Mol Cell,
16,
761-775.
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PDB code:
|
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E.J.Helmreich
(2004).
Structural flexibility of small GTPases. Can it explain their functional versatility?
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Biol Chem,
385,
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L.Xu,
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Nucleocytoplasmic shuttling of signal transducers.
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Nat Rev Mol Cell Biol,
5,
209-219.
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M.Dlakić,
and
D.Tollervey
(2004).
The Noc proteins involved in ribosome synthesis and export contain divergent HEAT repeats.
|
| |
RNA,
10,
351-354.
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|
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M.Lu,
J.M.Kinchen,
K.L.Rossman,
C.Grimsley,
C.deBakker,
E.Brugnera,
A.C.Tosello-Trampont,
L.B.Haney,
D.Klingele,
J.Sondek,
M.O.Hengartner,
and
K.S.Ravichandran
(2004).
PH domain of ELMO functions in trans to regulate Rac activation via Dock180.
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Nat Struct Mol Biol,
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756-762.
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M.N.Offman,
R.N.Nurtdinov,
M.S.Gelfand,
and
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(2004).
No statistical support for correlation between the positions of protein interaction sites and alternatively spliced regions.
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| |
BMC Bioinformatics,
5,
41.
|
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M.Oeffinger,
M.Dlakic,
and
D.Tollervey
(2004).
A pre-ribosome-associated HEAT-repeat protein is required for export of both ribosomal subunits.
|
| |
Genes Dev,
18,
196-209.
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N.Fukuhara,
E.Fernandez,
J.Ebert,
E.Conti,
and
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(2004).
Conformational variability of nucleo-cytoplasmic transport factors.
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J Biol Chem,
279,
2176-2181.
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R.Nevo,
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Direct discrimination between models of protein activation by single-molecule force measurements.
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Biophys J,
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Y.Matsuura,
and
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(2004).
Structural basis for the assembly of a nuclear export complex.
|
| |
Nature,
432,
872-877.
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|
PDB code:
|
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|
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
|
');
}
}
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