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PDBsum entry 4om2
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Transcription, DNA binding
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PDB id
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4om2
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PDB id:
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| Name: |
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Transcription, DNA binding
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Title:
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Crystal structure of tle1 n-terminal q-domain residues 1-156
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Structure:
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Transducin-like enhancer protein 1. Chain: a, b, c, d. Fragment: tle q-domain (unp residues 1-156). Synonym: e(sp1) homolog, enhancer of split groucho-like protein 1, esg1. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: tle, tle1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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4.00Å
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R-factor:
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0.294
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R-free:
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0.347
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Authors:
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J.V.Chodaparambil,W.I.Weis
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Key ref:
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J.V.Chodaparambil
et al.
(2014).
Molecular functions of the TLE tetramerization domain in Wnt target gene repression.
Embo J,
33,
719-731.
PubMed id:
DOI:
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Date:
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25-Jan-14
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Release date:
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09-Apr-14
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PROCHECK
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Headers
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References
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Q04724
(TLE1_HUMAN) -
Transducin-like enhancer protein 1 from Homo sapiens
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Seq:
Struc:
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770 a.a.
112 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Embo J
33:719-731
(2014)
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PubMed id:
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Molecular functions of the TLE tetramerization domain in Wnt target gene repression.
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J.V.Chodaparambil,
K.T.Pate,
M.R.Hepler,
B.P.Tsai,
U.M.Muthurajan,
K.Luger,
M.L.Waterman,
W.I.Weis.
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ABSTRACT
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Wnt signaling activates target genes by promoting association of the
co-activator β-catenin with TCF/LEF transcription factors. In the absence of
β-catenin, target genes are silenced by TCF-mediated recruitment of TLE/Groucho
proteins, but the molecular basis for TLE/TCF-dependent repression is unclear.
We describe the unusual three-dimensional structure of the N-terminal Q domain
of TLE1 that mediates tetramerization and binds to TCFs. We find that
differences in repression potential of TCF/LEFs correlates with their affinities
for TLE-Q, rather than direct competition between β-catenin and TLE for TCFs as
part of an activation-repression switch. Structure-based mutation of the TLE
tetramer interface shows that dimers cannot mediate repression, even though they
bind to TCFs with the same affinity as tetramers. Furthermore, the TLE Q
tetramer, not the dimer, binds to chromatin, specifically to K20 methylated
histone H4 tails, suggesting that the TCF/TLE tetramer complex promotes
structural transitions of chromatin to mediate repression.
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Links
