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PDBsum entry 2ac0
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Apoptosis/DNA
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PDB id
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2ac0
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References listed in PDB file
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Key reference
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Title
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Structural basis of DNA recognition by p53 tetramers.
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Authors
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M.Kitayner,
H.Rozenberg,
N.Kessler,
D.Rabinovich,
L.Shaulov,
T.E.Haran,
Z.Shakked.
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Ref.
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Mol Cell, 2006,
22,
741-753.
[DOI no: ]
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PubMed id
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Abstract
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The tumor-suppressor protein p53 is among the most effective of the cell's
natural defenses against cancer. In response to cellular stress, p53 binds as a
tetramer to diverse DNA targets containing two decameric half-sites, thereby
activating the expression of genes involved in cell-cycle arrest or apoptosis.
Here we present high-resolution crystal structures of sequence-specific
complexes between the core domain of human p53 and different DNA half-sites. In
all structures, four p53 molecules self-assemble on two DNA half-sites to form a
tetramer that is a dimer of dimers, stabilized by protein-protein and
base-stacking interactions. The protein-DNA interface varies as a function of
the specific base sequence in correlation with the measured binding affinities
of the complexes. The new data establish a structural framework for
understanding the mechanisms of specificity, affinity, and cooperativity of DNA
binding by p53 and suggest a model for its regulation by regions outside the
sequence-specific DNA binding domain.
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Figure 2.
Figure 2. Stereo Views of the Symmetrical Protein-Protein
Interface
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Figure 7.
Figure 7. A Model for Full-Length p53 Tetramer Bound to DNA
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2006,
22,
741-753)
copyright 2006.
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