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PDBsum entry 2grc
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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1.5 a structure of bromodomain from human brg1 protein, a central atpase of swi/snf remodeling complex
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Structure:
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Probable global transcription activator snf2l4. Chain: a. Fragment: bromodomain, residues 1448-1575. Synonym: atp- dependent helicase smarca4, snf2-beta, brg-1 protein, mitotic growth and transcription activator, brahma protein homolog 1, swi/snf-related matrix-associated actin-dependent regulator of chromatin subfamily a member 4. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: smarca4, brg1, snf2b, snf2l4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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1.50Å
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R-factor:
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0.243
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R-free:
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0.264
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Authors:
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M.Singh,G.M.Popowicz,M.Krajewski,T.A.Holak
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Key ref:
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M.Singh
et al.
(2007).
Structural ramification for acetyl-lysine recognition by the bromodomain of human BRG1 protein, a central ATPase of the SWI/SNF remodeling complex.
Chembiochem,
8,
1308-1316.
PubMed id:
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Date:
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24-Apr-06
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Release date:
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08-May-07
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PROCHECK
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Headers
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References
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P51532
(SMCA4_HUMAN) -
Transcription activator BRG1 from Homo sapiens
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Seq:
Struc:
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1647 a.a.
121 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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Chembiochem
8:1308-1316
(2007)
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PubMed id:
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Structural ramification for acetyl-lysine recognition by the bromodomain of human BRG1 protein, a central ATPase of the SWI/SNF remodeling complex.
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M.Singh,
G.M.Popowicz,
M.Krajewski,
T.A.Holak.
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ABSTRACT
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Bromodomains represent an extensive family of evolutionarily conserved domains
that are found in many chromatin-associated proteins such as histone
acetyltransferases (HAT) and subunits of ATP-dependent chromatin-remodeling
complexes. These domains are associated with acetylated lysine residues that
bind both in vivo and in vitro; for example, they bind to the N-acetylated
lysines of the histone tail of nucleosomes. In this report, we determined the
structure of the bromodomain from human brahma-related gene 1 (BRG1) protein, a
subunit of an ATP-dependent switching/sucrose nonfermenting (SWI/SNF) remodeling
complex, and have also characterized its in vitro interaction with N-acetylated
lysine peptides from histones. In addition to a typical all-alpha-helical fold
that was observed in the bromodomains, we observed for the first time a small
beta-sheet in the ZA loop region of the BRG1 protein. The BRG1 bromodomain
exhibited binding, albeit weak, to acetylated peptides that were derived from
histones H3 and H4. We have compared the acetyl-lysine binding sites of BRG1
bromodomain with the yGCN5 (general control of amino acid biosynthesis). By
modeling the acetylated-lysine peptide into the BRG1 bromodomain structure, we
were able to explain the weak binding of acetylated-lysine peptides to this
bromodomain.
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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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K.L.Yap,
and
M.M.Zhou
(2010).
Keeping it in the family: diverse histone recognition by conserved structural folds.
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Crit Rev Biochem Mol Biol,
45,
488-505.
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S.M.Cohen,
P.D.Chastain,
G.B.Rosson,
B.S.Groh,
B.E.Weissman,
D.G.Kaufman,
and
S.J.Bultman
(2010).
BRG1 co-localizes with DNA replication factors and is required for efficient replication fork progression.
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Nucleic Acids Res,
38,
6906-6919.
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X.Lu,
and
S.J.Triezenberg
(2010).
Chromatin assembly on herpes simplex virus genomes during lytic infection.
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Biochim Biophys Acta,
1799,
217-222.
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Y.Cao,
T.Vo,
G.Millien,
J.B.Tagne,
D.Kotton,
R.J.Mason,
M.C.Williams,
and
M.I.Ramirez
(2010).
Epigenetic mechanisms modulate thyroid transcription factor 1-mediated transcription of the surfactant protein B gene.
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J Biol Chem,
285,
2152-2164.
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G.P.Vicent,
R.Zaurin,
A.S.Nacht,
A.Li,
J.Font-Mateu,
F.Le Dily,
M.Vermeulen,
M.Mann,
and
M.Beato
(2009).
Two chromatin remodeling activities cooperate during activation of hormone responsive promoters.
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PLoS Genet,
5,
e1000567.
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J.J.van Vugt,
M.de Jager,
M.Murawska,
A.Brehm,
J.van Noort,
and
C.Logie
(2009).
Multiple aspects of ATP-dependent nucleosome translocation by RSC and Mi-2 are directed by the underlying DNA sequence.
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PLoS One,
4,
e6345.
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J.K.Choi,
and
L.J.Howe
(2009).
Histone acetylation: truth of consequences?
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Biochem Cell Biol,
87,
139-150.
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N.S.Kenneth,
S.Mudie,
P.van Uden,
and
S.Rocha
(2009).
SWI/SNF Regulates the Cellular Response to Hypoxia.
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J Biol Chem,
284,
4123-4131.
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R.Sanchez,
and
M.M.Zhou
(2009).
The role of human bromodomains in chromatin biology and gene transcription.
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Curr Opin Drug Discov Devel,
12,
659-665.
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S.Reuse,
M.Calao,
K.Kabeya,
A.Guiguen,
J.S.Gatot,
V.Quivy,
C.Vanhulle,
A.Lamine,
D.Vaira,
D.Demonte,
V.Martinelli,
E.Veithen,
T.Cherrier,
V.Avettand,
S.Poutrel,
J.Piette,
Y.de Launoit,
M.Moutschen,
A.Burny,
C.Rouzioux,
S.De Wit,
G.Herbein,
O.Rohr,
Y.Collette,
O.Lambotte,
N.Clumeck,
and
C.Van Lint
(2009).
Synergistic activation of HIV-1 expression by deacetylase inhibitors and prostratin: implications for treatment of latent infection.
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PLoS One,
4,
e6093.
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T.M.Becker,
S.Haferkamp,
M.K.Dijkstra,
L.L.Scurr,
M.Frausto,
E.Diefenbach,
R.A.Scolyer,
D.N.Reisman,
G.J.Mann,
R.F.Kefford,
and
H.Rizos
(2009).
The chromatin remodelling factor BRG1 is a novel binding partner of the tumor suppressor p16INK4a.
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Mol Cancer,
8,
4.
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K.W.Trotter,
and
T.K.Archer
(2008).
The BRG1 transcriptional coregulator.
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Nucl Recept Signal,
6,
e004.
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H.Huang,
J.Zhang,
W.Shen,
X.Wang,
J.Wu,
J.Wu,
and
Y.Shi
(2007).
Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails.
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BMC Struct Biol,
7,
57.
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S.Lall
(2007).
Primers on chromatin.
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Nat Struct Mol Biol,
14,
1110-1115.
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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.
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Links
