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PDBsum entry 2mbh
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Transcription
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PDB id
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2mbh
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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 characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-Specific factor eklf.
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Authors
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L.Raiola,
M.Lussier-Price,
D.Gagnon,
J.Lafrance-Vanasse,
X.Mascle,
G.Arseneault,
P.Legault,
J.Archambault,
J.G.Omichinski.
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Ref.
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Structure, 2013,
21,
2014-2024.
[DOI no: ]
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PubMed id
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Abstract
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Like other acidic transactivation domains (TAD), the minimal TAD from the
erythroid-specific transcription factor EKLF (EKLFTAD) has been shown to
contribute both to its transcriptional activity as well as to its
ubiquitin(UBI)-mediated degradation. In this article, we examine the
activation-degradation role of the acidic TAD of EKLF and demonstrate that the
first 40 residues (EKLFTAD1) within this region form a noncovalent interaction
with UBI. Nuclear magnetic resonance (NMR) structural studies of an EKLFTAD1-UBI
complex show that EKLFTAD1 adopts a 14-residue α helix that forms the
recognition interface with UBI in a similar manner as the UBI-interacting helix
of Rabex5. We also identify a similar interaction between UBI and the
activation-degradation region of SREBP1a, but not with the
activation-degradation regions of p53, GAL4, and VP16. These results suggest
that select activation-degradation regions like the ones found in EKLF and
SREBP1a function in part through their ability to form noncovalent interactions
with UBI.
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