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PDBsum entry 3wts
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Transcription/DNA
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PDB id
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3wts
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Contents |
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119 a.a.
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130 a.a.
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118 a.a.
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101 a.a.
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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 novel allosteric mechanism on protein-Dna interactions underlying the phosphorylation-Dependent regulation of ets1 target gene expressions.
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Authors
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M.Shiina,
K.Hamada,
T.Inoue-Bungo,
M.Shimamura,
A.Uchiyama,
S.Baba,
K.Sato,
M.Yamamoto,
K.Ogata.
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Ref.
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J Mol Biol, 2015,
427,
1655-1669.
[DOI no: ]
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PubMed id
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Abstract
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Cooperative assemblies of transcription factors (TFs) on target gene enhancers
coordinate cell proliferation, fate specification, and differentiation through
precise and complicated transcriptional mechanisms. Chemical modifications, such
as phosphorylation, of TFs induced by cell signaling further modulate the
dynamic cooperativity of TFs. In this study, we found that various
Ets1-containing TF-DNA complexes respond differently to calcium-induced
phosphorylation of Ets1, which is known to inhibit Ets1-DNA binding.
Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the
TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1
and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated
Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1
target gene enhancers including mb-1 and stromelysin-1. This study provides a
structure-based model for cell-signaling-dependent regulation of target genes,
mediated via chemical modification of TFs.
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