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PDBsum entry 1cs3
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Transcription
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PDB id
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1cs3
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Contents |
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* Residue conservation analysis
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Cancer Res
59:5275-5282
(1999)
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PubMed id:
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Structure-function studies of the BTB/POZ transcriptional repression domain from the promyelocytic leukemia zinc finger oncoprotein.
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X.Li,
H.Peng,
D.C.Schultz,
J.M.Lopez-Guisa,
F.J.Rauscher,
R.Marmorstein.
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ABSTRACT
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The evolutionarily conserved BTB/POZ domain from the promyelocytic leukemia zinc
finger (PLZF) oncoprotein mediates transcriptional repression through the
recruitment of corepressor proteins containing histone deacetylases in acute
promyelocytic leukemia. We have determined the 2.0 A crystal structure of the
BTB/POZ domain from PLZF (PLZF-BTB/POZ), and have carried out biochemical
analysis of PLZF-BTB/POZ harboring site-directed mutations to probe
structure-function relationships. The structure reveals a novel alpha/beta
homodimeric fold in which dimer interactions occur along two surfaces of the
protein subunits. The conservation of BTB/POZ domain residues at the core of the
protomers and at the dimer interface implies an analogous fold and dimerization
mode for BTB/POZ domains from otherwise functionally unrelated proteins.
Unexpectedly, the BTB/POZ domain forms dimer-dimer interactions in the crystals,
suggesting a mode for higher-order protein oligomerization for BTB/POZ-mediated
transcriptional repression. Biochemical characterization of PLZF-BTB/POZ
harboring mutations in conserved residues involved in protein dimerization
reveals that the integrity of the dimer interface is exquisitely sensitive to
mutation and that dimer formation is required for wild-type levels of
transcriptional repression. Interestingly, similar mutational analysis of
residues within a pronounced protein cleft along the dimer interface, which had
been implicated previously for interaction with corepressors, has negligible
effects on dimerization or transcriptional repression. Together, these studies
form a structure-function framework for understanding BTB/POZ-mediated
oligomerization and transcriptional repression properties.
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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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P.H.Wu,
S.H.Hung,
T.Ren,
I.e.M.Shih,
and
Y.Tseng
(2011).
Cell cycle-dependent alteration in NAC1 nuclear body dynamics and morphology.
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Phys Biol,
8,
015005.
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S.A.Devaney,
S.E.Mate,
J.M.Devaney,
and
E.P.Hoffman
(2011).
Characterization of the ZBTB42 gene in humans and mice.
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Hum Genet,
129,
433-441.
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I.S.Dementieva,
V.Tereshko,
Z.A.McCrossan,
E.Solomaha,
D.Araki,
C.Xu,
N.Grigorieff,
and
S.A.Goldstein
(2009).
Pentameric assembly of potassium channel tetramerization domain-containing protein 5.
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J Mol Biol,
387,
175-191.
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PDB codes:
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N.Ito,
M.Watanabe-Matsui,
K.Igarashi,
and
K.Murayama
(2009).
Crystal structure of the Bach1 BTB domain and its regulation of homodimerization.
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Genes Cells,
14,
167-178.
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X.Ding,
C.Luo,
J.Zhou,
Y.Zhong,
X.Hu,
F.Zhou,
K.Ren,
L.Gan,
A.He,
J.Zhu,
X.Gao,
and
J.Zhang
(2009).
The interaction of KCTD1 with transcription factor AP-2alpha inhibits its transactivation.
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J Cell Biochem,
106,
285-295.
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B.A.Wilton,
S.Campbell,
N.Van Buuren,
R.Garneau,
M.Furukawa,
Y.Xiong,
and
M.Barry
(2008).
Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases.
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Virology,
374,
82-99.
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M.A.Stead,
G.O.Rosbrook,
J.M.Hadden,
C.H.Trinh,
S.B.Carr,
and
S.C.Wright
(2008).
Structure of the wild-type human BCL6 POZ domain.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
1101-1104.
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PDB code:
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X.F.Ding,
C.Luo,
K.Q.Ren,
J.Zhang,
J.L.Zhou,
X.Hu,
R.S.Liu,
Y.Wang,
X.Gao,
and
J.Zhang
(2008).
Characterization and expression of a human KCTD1 gene containing the BTB domain, which mediates transcriptional repression and homomeric interactions.
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DNA Cell Biol,
27,
257-265.
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L.Korutla,
R.Degnan,
P.Wang,
and
S.A.Mackler
(2007).
NAC1, a cocaine-regulated POZ/BTB protein interacts with CoREST.
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J Neurochem,
101,
611-618.
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P.J.Stogios,
L.Chen,
and
G.G.Privé
(2007).
Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator.
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Protein Sci,
16,
336-342.
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PDB code:
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F.Schoenen,
and
B.Wirth
(2006).
The zinc finger protein ZNF297B interacts with BDP1, a subunit of TFIIIB.
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Biol Chem,
387,
277-284.
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R.Perez-Torrado,
D.Yamada,
and
P.A.Defossez
(2006).
Born to bind: the BTB protein-protein interaction domain.
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Bioessays,
28,
1194-1202.
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A.J.Edgar,
S.L.Dover,
M.N.Lodrick,
I.J.McKay,
F.J.Hughes,
and
W.Turner
(2005).
Bone morphogenetic protein-2 induces expression of murine zinc finger transcription factor ZNF450.
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J Cell Biochem,
94,
202-215.
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J.Zhou,
X.Hu,
X.Xiong,
X.Liu,
Y.Liu,
K.Ren,
T.Jiang,
X.Hu,
and
J.Zhang
(2005).
Cloning of two rat PDIP1 related genes and their interactions with proliferating cell nuclear antigen.
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J Exp Zoolog A Comp Exp Biol,
303,
227-240.
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P.J.Stogios,
G.S.Downs,
J.J.Jauhal,
S.K.Nandra,
and
G.G.Privé
(2005).
Sequence and structural analysis of BTB domain proteins.
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Genome Biol,
6,
R82.
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S.Luke-Glaser,
L.Pintard,
C.Lu,
P.E.Mains,
and
M.Peter
(2005).
The BTB protein MEL-26 promotes cytokinesis in C. elegans by a CUL-3-independent mechanism.
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Curr Biol,
15,
1605-1615.
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K.F.Ahmad,
A.Melnick,
S.Lax,
D.Bouchard,
J.Liu,
C.L.Kiang,
S.Mayer,
S.Takahashi,
J.D.Licht,
and
G.G.Privé
(2003).
Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain.
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Mol Cell,
12,
1551-1564.
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PDB codes:
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R.Geyer,
S.Wee,
S.Anderson,
J.Yates,
and
D.A.Wolf
(2003).
BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases.
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Mol Cell,
12,
783-790.
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A.Melnick,
G.Carlile,
K.F.Ahmad,
C.L.Kiang,
C.Corcoran,
V.Bardwell,
G.G.Prive,
and
J.D.Licht
(2002).
Critical residues within the BTB domain of PLZF and Bcl-6 modulate interaction with corepressors.
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Mol Cell Biol,
22,
1804-1818.
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L.Xu,
L.Yang,
K.Hashimoto,
M.Anderson,
G.Kohlhagen,
Y.Pommier,
and
P.D'Arpa
(2002).
Characterization of BTBD1 and BTBD2, two similar BTB-domain-containing Kelch-like proteins that interact with Topoisomerase I.
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BMC Genomics,
3,
1.
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S.Li,
C.Xu,
and
R.W.Carthew
(2002).
Phyllopod acts as an adaptor protein to link the sina ubiquitin ligase to the substrate protein tramtrack.
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Mol Cell Biol,
22,
6854-6865.
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S.Pagans,
M.Ortiz-Lombardía,
M.L.Espinás,
J.Bernués,
and
F.Azorín
(2002).
The Drosophila transcription factor tramtrack (TTK) interacts with Trithorax-like (GAGA) and represses GAGA-mediated activation.
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Nucleic Acids Res,
30,
4406-4413.
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T.Collins,
J.R.Stone,
and
A.J.Williams
(2001).
All in the family: the BTB/POZ, KRAB, and SCAN domains.
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Mol Cell Biol,
21,
3609-3615.
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A.Melnick,
K.F.Ahmad,
S.Arai,
A.Polinger,
H.Ball,
K.L.Borden,
G.W.Carlile,
G.G.Prive,
and
J.D.Licht
(2000).
In-depth mutational analysis of the promyelocytic leukemia zinc finger BTB/POZ domain reveals motifs and residues required for biological and transcriptional functions.
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Mol Cell Biol,
20,
6550-6567.
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D.Read,
M.J.Butte,
A.F.Dernburg,
M.Frasch,
and
T.B.Kornberg
(2000).
Functional studies of the BTB domain in the Drosophila GAGA and Mod(mdg4) proteins.
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Nucleic Acids Res,
28,
3864-3870.
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K.D.Huynh,
W.Fischle,
E.Verdin,
and
V.J.Bardwell
(2000).
BCoR, a novel corepressor involved in BCL-6 repression.
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Genes Dev,
14,
1810-1823.
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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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