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PDBsum entry 3o33
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Transcription
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PDB id
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3o33
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Contents |
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* Residue conservation analysis
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PDB id:
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Transcription
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Title:
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Crystal structure of trim24 phd-bromo in the free state
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Structure:
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Transcription intermediary factor 1-alpha. Chain: a, b, c, d. Fragment: unp residues 824-1006. Synonym: tif1-alpha, tripartite motif-containing protein 24, ring finger protein 82. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: trim24, rnf82, tif1, tif1a. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.00Å
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R-factor:
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0.221
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R-free:
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0.244
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Authors:
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Z.Wang,D.J.Patel
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Key ref:
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W.W.Tsai
et al.
(2010).
TRIM24 links a non-canonical histone signature to breast cancer.
Nature,
468,
927-932.
PubMed id:
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Date:
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23-Jul-10
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Release date:
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15-Dec-10
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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.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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Nature
468:927-932
(2010)
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PubMed id:
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TRIM24 links a non-canonical histone signature to breast cancer.
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W.W.Tsai,
Z.Wang,
T.T.Yiu,
K.C.Akdemir,
W.Xia,
S.Winter,
C.Y.Tsai,
X.Shi,
D.Schwarzer,
W.Plunkett,
B.Aronow,
O.Gozani,
W.Fischle,
M.C.Hung,
D.J.Patel,
M.C.Barton.
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ABSTRACT
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Recognition of modified histone species by distinct structural domains within
'reader' proteins plays a critical role in the regulation of gene expression.
Readers that simultaneously recognize histones with multiple marks allow
transduction of complex chromatin modification patterns into specific biological
outcomes. Here we report that chromatin regulator tripartite motif-containing 24
(TRIM24) functions in humans as a reader of dual histone marks by means of
tandem plant homeodomain (PHD) and bromodomain (Bromo) regions. The
three-dimensional structure of the PHD-Bromo region of TRIM24 revealed a single
functional unit for combinatorial recognition of unmodified H3K4 (that is,
histone H3 unmodified at lysine 4, H3K4me0) and acetylated H3K23 (histone H3
acetylated at lysine 23, H3K23ac) within the same histone tail. TRIM24 binds
chromatin and oestrogen receptor to activate oestrogen-dependent genes
associated with cellular proliferation and tumour development. Aberrant
expression of TRIM24 negatively correlates with survival of breast cancer
patients. The PHD-Bromo of TRIM24 provides a structural rationale for chromatin
activation through a non-canonical histone signature, establishing a new route
by which chromatin readers may influence cancer pathogenesis.
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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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C.A.Musselman,
M.E.Lalonde,
J.Côté,
and
T.G.Kutateladze
(2012).
Perceiving the epigenetic landscape through histone readers.
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Nat Struct Mol Biol,
19,
1218-1227.
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E.L.Greer,
and
Y.Shi
(2012).
Histone methylation: a dynamic mark in health, disease and inheritance.
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Nat Rev Genet,
13,
343-357.
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K.E.Gardner,
C.D.Allis,
and
B.D.Strahl
(2011).
OPERating ON Chromatin, a Colorful Language where Context Matters.
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J Mol Biol,
409,
36-46.
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S.Eustermann,
J.C.Yang,
M.J.Law,
R.Amos,
L.M.Chapman,
C.Jelinska,
D.Garrick,
D.Clynes,
R.J.Gibbons,
D.Rhodes,
D.R.Higgs,
and
D.Neuhaus
(2011).
Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin.
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Nat Struct Mol Biol,
18,
777-782.
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PDB code:
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S.Hatakeyama
(2011).
TRIM proteins and cancer.
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Nat Rev Cancer,
11,
792-804.
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S.Iwase,
B.Xiang,
S.Ghosh,
T.Ren,
P.W.Lewis,
J.C.Cochrane,
C.D.Allis,
D.J.Picketts,
D.J.Patel,
H.Li,
and
Y.Shi
(2011).
ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome.
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Nat Struct Mol Biol,
18,
769-776.
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PDB codes:
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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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Links
