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* Residue conservation analysis
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PDB id:
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Nuclear import
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Title:
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Crystal structure of yeast karyopherin (importin) alpha in complex with a nup2p n-terminal fragment
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Structure:
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Importin alpha subunit. Chain: a, b. Fragment: armadillo repeat domain, residues 88-530. Synonym: kap60p, karyopherin alpha subunit, serine-rich RNA polymerase i suppressor protein. Engineered: yes. Mutation: yes. Nucleoporin nup2. Chain: c, d.
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Biol. unit:
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Dimer (from PDB file)
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Resolution:
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2.60Å
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R-factor:
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0.218
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R-free:
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0.257
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Authors:
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Y.Matsuura,A.Lange,M.T.Harreman,A.H.Corbett,M.Stewart
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Key ref:
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Y.Matsuura
et al.
(2003).
Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import.
Embo J,
22,
5358-5369.
PubMed id:
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Date:
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03-Sep-03
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Release date:
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16-Oct-03
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B, C, D:
E.C.?
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Embo J
22:5358-5369
(2003)
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PubMed id:
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Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import.
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Y.Matsuura,
A.Lange,
M.T.Harreman,
A.H.Corbett,
M.Stewart.
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ABSTRACT
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The yeast nucleoporin Nup2p is associated primarily with the nuclear basket of
nuclear pore complexes and is required for efficient
importin-alpha:beta-mediated nuclear protein import as well as efficient nuclear
export of Kap60p/importin-alpha. Residues 1-51 of Nup2p bind tightly to Kap60p
and are required for Nup2p function in vivo. We have determined the 2.6 A
resolution crystal structure of a complex between this region of Nup2p and the
armadillo repeat domain of Kap60p. Nup2p binds along the inner concave groove of
Kap60p, but its interaction interface is different from that employed for
nuclear localization signal (NLS) recognition although there is some overlap
between them. Nup2p binds Kap60p more strongly than NLSs and accelerates release
of NLSs from Kap60p. Nup2p itself is released from Kap60p by Cse1p:RanGTP only
in the presence of the importin-beta binding (IBB) domain of Kap60p. These data
indicate that Nup2p increases the overall rate of nuclear trafficking by
coordinating nuclear import termination and importin recycling as a concerted
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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A.Giesecke,
and
M.Stewart
(2010).
Novel binding of the mitotic regulator TPX2 (target protein for Xenopus kinesin-like protein 2) to importin-alpha.
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J Biol Chem,
285,
17628-17635.
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PDB code:
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H.Kosako,
and
N.Imamoto
(2010).
Phosphorylation of nucleoporins: Signal transduction-mediated regulation of their interaction with nuclear transport receptors.
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Nucleus,
1,
309-313.
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Y.Ogawa,
Y.Miyamoto,
M.Asally,
M.Oka,
Y.Yasuda,
and
Y.Yoneda
(2010).
Two isoforms of Npap60 (Nup50) differentially regulate nuclear protein import.
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Mol Biol Cell,
21,
630-638.
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C.P.De Souza,
and
S.A.Osmani
(2009).
Double duty for nuclear proteins--the price of more open forms of mitosis.
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Trends Genet,
25,
545-554.
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K.F.Pulliam,
M.B.Fasken,
L.M.McLane,
J.V.Pulliam,
and
A.H.Corbett
(2009).
The Classical Nuclear Localization Signal Receptor, Importin-{alpha}, Is Required for Efficient Transition Through the G1/S Stage of the Cell Cycle in Saccharomyces cerevisiae.
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Genetics,
181,
105-118.
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N.Freitas,
and
C.Cunha
(2009).
Mechanisms and signals for the nuclear import of proteins.
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Curr Genomics,
10,
550-557.
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C.Sun,
W.Yang,
L.C.Tu,
and
S.M.Musser
(2008).
Single-molecule measurements of importin alpha/cargo complex dissociation at the nuclear pore.
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Proc Natl Acad Sci U S A,
105,
8613-8618.
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G.Bird,
M.O'Donnell,
J.Moroianu,
and
R.L.Garcea
(2008).
Possible role for cellular karyopherins in regulating polyomavirus and papillomavirus capsid assembly.
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J Virol,
82,
9848-9857.
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G.Mitrousis,
A.S.Olia,
N.Walker-Kopp,
and
G.Cingolani
(2008).
Molecular basis for the recognition of snurportin 1 by importin beta.
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J Biol Chem,
283,
7877-7884.
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PDB codes:
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M.M.Pradeepa,
S.Manjunatha,
V.Sathish,
S.Agrawal,
and
M.R.Rao
(2008).
Involvement of importin-4 in the transport of transition protein 2 into the spermatid nucleus.
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Mol Cell Biol,
28,
4331-4341.
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W.Yao,
M.Lutzmann,
and
E.Hurt
(2008).
A versatile interaction platform on the Mex67-Mtr2 receptor creates an overlap between mRNA and ribosome export.
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EMBO J,
27,
6.
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Y.Shen,
K.K.Hixson,
N.Tolić,
D.G.Camp,
S.O.Purvine,
R.J.Moore,
and
R.D.Smith
(2008).
Mass spectrometry analysis of proteome-wide proteolytic post-translational degradation of proteins.
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Anal Chem,
80,
5819-5828.
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A.Lange,
R.E.Mills,
C.J.Lange,
M.Stewart,
S.E.Devine,
and
A.H.Corbett
(2007).
Classical nuclear localization signals: definition, function, and interaction with importin alpha.
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J Biol Chem,
282,
5101-5105.
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A.Lewis,
R.Felberbaum,
and
M.Hochstrasser
(2007).
A nuclear envelope protein linking nuclear pore basket assembly, SUMO protease regulation, and mRNA surveillance.
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J Cell Biol,
178,
813-827.
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C.P.Lusk,
G.Blobel,
and
M.C.King
(2007).
Highway to the inner nuclear membrane: rules for the road.
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Nat Rev Mol Cell Biol,
8,
414-420.
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L.J.Terry,
and
S.R.Wente
(2007).
Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex.
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J Cell Biol,
178,
1121-1132.
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M.A.Brykailo,
L.M.McLane,
J.Fridovich-Keil,
and
A.H.Corbett
(2007).
Analysis of a predicted nuclear localization signal: implications for the intracellular localization and function of the Saccharomyces cerevisiae RNA-binding protein Scp160.
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Nucleic Acids Res,
35,
6862-6869.
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M.Stewart
(2007).
Molecular mechanism of the nuclear protein import cycle.
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Nat Rev Mol Cell Biol,
8,
195-208.
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T.A.Isgro,
and
K.Schulten
(2007).
Cse1p-binding dynamics reveal a binding pattern for FG-repeat nucleoporins on transport receptors.
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Structure,
15,
977-991.
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A.E.Hodel,
M.T.Harreman,
K.F.Pulliam,
M.E.Harben,
J.S.Holmes,
M.R.Hodel,
K.M.Berland,
and
A.H.Corbett
(2006).
Nuclear localization signal receptor affinity correlates with in vivo localization in Saccharomyces cerevisiae.
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J Biol Chem,
281,
23545-23556.
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A.H.Osmani,
J.Davies,
H.L.Liu,
A.Nile,
and
S.A.Osmani
(2006).
Systematic deletion and mitotic localization of the nuclear pore complex proteins of Aspergillus nidulans.
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Mol Biol Cell,
17,
4946-4961.
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A.S.Madrid,
and
K.Weis
(2006).
Nuclear transport is becoming crystal clear.
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Chromosoma,
115,
98.
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R.Y.Lim,
and
B.Fahrenkrog
(2006).
The nuclear pore complex up close.
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Curr Opin Cell Biol,
18,
342-347.
|
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|
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D.R.Littler,
N.N.Assaad,
S.J.Harrop,
L.J.Brown,
G.J.Pankhurst,
P.Luciani,
M.I.Aguilar,
M.Mazzanti,
M.A.Berryman,
S.N.Breit,
and
P.M.Curmi
(2005).
Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4.
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FEBS J,
272,
4996-5007.
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PDB code:
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E.J.Blink,
Z.Jiansheng,
W.Hu,
S.T.Calanni,
J.A.Trapani,
P.I.Bird,
and
D.A.Jans
(2005).
Interaction of the nuclear localizing cytolytic granule serine protease granzyme B with importin alpha or beta: modulation by the serpin inhibitor PI-9.
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J Cell Biochem,
95,
598-610.
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|
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S.J.Lee,
Y.Matsuura,
S.M.Liu,
and
M.Stewart
(2005).
Structural basis for nuclear import complex dissociation by RanGTP.
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Nature,
435,
693-696.
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PDB code:
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Y.Matsuura,
and
M.Stewart
(2005).
Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling.
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EMBO J,
24,
3681-3689.
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PDB codes:
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C.P.Lusk,
T.Makhnevych,
and
R.W.Wozniak
(2004).
New ways to skin a kap: mechanisms for controlling nuclear transport.
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Biochem Cell Biol,
82,
618-625.
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|
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D.S.Goldfarb,
A.H.Corbett,
D.A.Mason,
M.T.Harreman,
and
S.A.Adam
(2004).
Importin alpha: a multipurpose nuclear-transport receptor.
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Trends Cell Biol,
14,
505-514.
|
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|
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M.A.Powers,
and
M.Dasso
(2004).
Nuclear transport erupts on the slopes of Mount Etna.
|
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Nat Cell Biol,
6,
82-86.
|
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W.Wang,
X.Yang,
T.Kawai,
I.López de Silanes,
K.Mazan-Mamczarz,
P.Chen,
Y.M.Chook,
C.Quensel,
M.Köhler,
and
M.Gorospe
(2004).
AMP-activated protein kinase-regulated phosphorylation and acetylation of importin alpha1: involvement in the nuclear import of RNA-binding protein HuR.
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J Biol Chem,
279,
48376-48388.
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Y.Matsuura,
and
M.Stewart
(2004).
Structural basis for the assembly of a nuclear export complex.
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Nature,
432,
872-877.
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PDB code:
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M.Stewart
(2003).
Structural biology. Nuclear trafficking.
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Science,
302,
1513-1514.
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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
code is
shown on the right.
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}
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