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PDBsum entry 1jjs
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Transcription
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PDB id
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1jjs
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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A small domain of cbp/p300 binds diverse proteins: solution structure and functional studies.
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Authors
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C.H.Lin,
B.J.Hare,
G.Wagner,
S.C.Harrison,
T.Maniatis,
E.Fraenkel.
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Ref.
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Mol Cell, 2001,
8,
581-590.
[DOI no: ]
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PubMed id
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Abstract
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The transcriptional coactivators CBP and p300 are critical regulators of
metazoan gene expression. They associate with many different DNA-bound
transcription factors through small, conserved domains. We have identified a
compactly folded 46 residue domain in CBP and p300, the IRF-3 binding domain
(IBiD), and we have determined its structure by NMR. It has a helical framework
containing an apparently flexible polyglutamine loop that participates in ligand
binding. Spectroscopic data indicate that induced folding accompanies
association of IBiD with its partners, which exhibit no evident sequence
similarities. We demonstrate the significance both in vitro and in vivo of
interactions between IBiD and a number of diverse partners. Thus, IBiD is an
important contributor to signal integration by CBP and p300.
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Figure 5.
Figure 5. IRF-3, KSHV IRF-1, TIF-2, and E1A Compete for
Binding to IBiD(A) CAT reporter activity measured in extracts of
cells transfected with the indicated plasmids (E1A 12S WT or
H3N: 1 μg; IRF-3 E5: 0.5 μg and 1 μg; KSHV IRF-1: 0.5 μg and
1 μg) or infected with Sendai virus.(B) In vitro pull-down
analysis using immobilized IBiD showing the competition for
binding to IBiD between TIF-2 (cold) and either IRF-3 E5 or KSHV
IRF-1 (^35S-labeled). The percentages of IRF-3 E5 and KSHV IRF-1
that remained bound are shown.(C) CAT assays showing the
inhibitory effect of either WT or H3N E1A 12S on virus induction
of (PRDIII-I)[3]. Amounts of effector constructs transfected:
0.5 and 1 μg. Immunoblot analysis (inset) using an α-E1A
antibody (Santa Cruz) indicates the expression levels of these
E1A constructs.(D) CAT assays showing the inhibitory effect of
either WT or H3N E1A 12S, and KSHV IRF-1 on the transcription
driven by Gal4-IRF-3 E5. Amounts of effector constructs
transfected: Gal4-IRF-3 E5, 50 ng; viral gene constructs, 0.25,
0.5, and 1 μg
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Figure 6.
Figure 6. Flexible Domain Organization of CBP/p300Schematic
diagram illustrating how flexible tethers may permit CBP/p300
molecules to adapt to different enhancers. Binding of ligands
can indirectly modify acetyltransferase activity by causing
domain rearrangements. Two mechanisms by which phosphorylation
of a ligand regulates its binding to CBP/p300 are also shown
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2001,
8,
581-590)
copyright 2001.
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