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PDBsum entry 1uuj
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Cell division
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PDB id
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1uuj
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Contents |
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* Residue conservation analysis
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PDB id:
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Cell division
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Title:
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N-terminal domain of lissencephaly-1 protein (lis-1)
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Structure:
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Platelet-activating factor acetylhydrolase ib alpha subunit. Chain: a, b, c, d. Fragment: n-terminal domain residues 1-85. Synonym: lissencephaly-1 protein, paf, paf-ah alpha, acetylhydrolase 45 kda subunit, paf-ah 45 kda subunit, pafah alpha, lis-1. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Organ: brain. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Dimer (from PDB file)
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Resolution:
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1.75Å
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R-factor:
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0.192
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R-free:
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0.246
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Authors:
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D.R.Cooper,M.H.Kim,Y.Devedjiev,U.Derewenda,Z.S.Derewenda
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Key ref:
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M.H.Kim
et al.
(2004).
The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications.
Structure,
12,
987-998.
PubMed id:
DOI:
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Date:
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22-Dec-03
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Release date:
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29-Jul-04
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PROCHECK
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Headers
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References
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P63005
(LIS1_MOUSE) -
Platelet-activating factor acetylhydrolase IB subunit beta from Mus musculus
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Seq:
Struc:
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410 a.a.
76 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Structure
12:987-998
(2004)
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PubMed id:
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The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications.
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M.H.Kim,
D.R.Cooper,
A.Oleksy,
Y.Devedjiev,
U.Derewenda,
O.Reiner,
J.Otlewski,
Z.S.Derewenda.
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ABSTRACT
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Mutations in the Lis1 gene result in lissencephaly (smooth brain), a
debilitating developmental syndrome caused by the impaired ability of
postmitotic neurons to migrate to their correct destination in the cerebral
cortex. Sequence similarities suggest that the LIS1 protein contains a
C-terminal seven-blade beta-propeller domain, while the structure of the
N-terminal fragment includes the LisH (Lis-homology) motif, a pattern found in
over 100 eukaryotic proteins with a hitherto unknown function. We present the
1.75 A resolution crystal structure of the N-terminal domain of mouse LIS1, and
we show that the LisH motif is a novel, thermodynamically very stable
dimerization domain. The structure explains the molecular basis of a low
severity form of lissencephaly.
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Selected figure(s)
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Figure 5.
Figure 5. The Coiled-Coil SegmentThe coiled coils of C/D
dimer are shown as helices extending from a surface of the LisH
domain. The hydrophobic residues of the heptad repeats are
shown. Surfaces were generated in GRASP (Nicholls et al., 1991).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
987-998)
copyright 2004.
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Figure was
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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J.Oberoi,
L.Fairall,
P.J.Watson,
J.C.Yang,
Z.Czimmerer,
T.Kampmann,
B.T.Goult,
J.A.Greenwood,
J.T.Gooch,
B.C.Kallenberger,
L.Nagy,
D.Neuhaus,
and
J.W.Schwabe
(2011).
Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery.
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Nat Struct Mol Biol,
18,
177-184.
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PDB codes:
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C.Su,
Y.Li,
Y.Lu,
and
J.Chen
(2009).
Mss11, a transcriptional activator, is required for hyphal development in Candida albicans.
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Eukaryot Cell,
8,
1780-1791.
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J.R.Kardon,
and
R.D.Vale
(2009).
Regulators of the cytoplasmic dynein motor.
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Nat Rev Mol Cell Biol,
10,
854-865.
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A.Akhmanova,
and
M.O.Steinmetz
(2008).
Tracking the ends: a dynamic protein network controls the fate of microtubule tips.
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Nat Rev Mol Cell Biol,
9,
309-322.
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D.A.Dansereau,
and
P.Lasko
(2008).
RanBPM regulates cell shape, arrangement, and capacity of the female germline stem cell niche in Drosophila melanogaster.
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J Cell Biol,
182,
963-977.
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H.Fujioka,
T.Ariga,
K.Horiuchi,
S.Ishikiriyama,
K.Oyama,
M.Otsu,
K.Kawashima,
Y.Yamamoto,
T.Sugihara,
and
Y.Sakiyama
(2008).
Detection of a novel silent deletion, a missense mutation and a nonsense mutation in TCOF1.
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Pediatr Int,
50,
806-809.
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K.Helmstaedt,
K.Laubinger,
K.Vosskuhl,
O.Bayram,
S.Busch,
M.Hoppert,
O.Valerius,
S.Seiler,
and
G.H.Braus
(2008).
The nuclear migration protein NUDF/LIS1 forms a complex with NUDC and BNFA at spindle pole bodies.
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Eukaryot Cell,
7,
1041-1052.
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M.Valiyaveettil,
A.A.Bentley,
P.Gursahaney,
R.Hussien,
R.Chakravarti,
N.Kureishy,
S.Prag,
and
J.C.Adams
(2008).
Novel role of the muskelin-RanBP9 complex as a nucleocytoplasmic mediator of cell morphology regulation.
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J Cell Biol,
182,
727-739.
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S.Hebbar,
M.T.Mesngon,
A.M.Guillotte,
B.Desai,
R.Ayala,
and
D.S.Smith
(2008).
Lis1 and Ndel1 influence the timing of nuclear envelope breakdown in neural stem cells.
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J Cell Biol,
182,
1063-1071.
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G.Giorgio,
M.Alfieri,
C.Prattichizzo,
A.Zullo,
S.Cairo,
and
B.Franco
(2007).
Functional characterization of the OFD1 protein reveals a nuclear localization and physical interaction with subunits of a chromatin remodeling Complex.
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Mol Biol Cell,
18,
4397-4404.
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N.Yamaguchi,
H.Koizumi,
J.Aoki,
Y.Natori,
K.Nishikawa,
Y.Natori,
Y.Takanezawa,
and
H.Arai
(2007).
Type I platelet-activating factor acetylhydrolase catalytic subunits over-expression induces pleiomorphic nuclei and centrosome amplification.
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Genes Cells,
12,
1153-1161.
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F.Cao,
S.Lane,
P.P.Raniga,
Y.Lu,
Z.Zhou,
K.Ramon,
J.Chen,
and
H.Liu
(2006).
The Flo8 transcription factor is essential for hyphal development and virulence in Candida albicans.
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Mol Biol Cell,
17,
295-307.
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S.Hafizi,
A.Gustafsson,
J.Stenhoff,
and
B.Dahlbäck
(2005).
The Ran binding protein RanBPM interacts with Axl and Sky receptor tyrosine kinases.
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Int J Biochem Cell Biol,
37,
2344-2356.
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C.Tarricone,
F.Perrina,
S.Monzani,
L.Massimiliano,
M.H.Kim,
Z.S.Derewenda,
S.Knapp,
L.H.Tsai,
and
A.Musacchio
(2004).
Coupling PAF signaling to dynein regulation: structure of LIS1 in complex with PAF-acetylhydrolase.
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Neuron,
44,
809-821.
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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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Links
