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PDBsum entry 1gxr
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Transcription
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PDB id
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1gxr
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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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Crystal structure of the c-Terminal wd40 repeat domain of the human groucho/tle1 transcriptional corepressor.
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Authors
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L.M.Pickles,
S.M.Roe,
E.J.Hemingway,
S.Stifani,
L.H.Pearl.
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Ref.
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Structure, 2002,
10,
751-761.
[DOI no: ]
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PubMed id
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Abstract
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Groucho (Gro)/TLE proteins are transcriptional corepressors that lack inherent
DNA binding but interact with DNA-bound transcription factors and histones, and
recruit histone deacetylases. Groucho-mediated repression is essential in
embryonic development and involved in regulation of Wnt signaling in adult
tissue. We have determined the 1.6 A crystal structure of a C-terminal fragment
of human Groucho/TLE1, comprising part of the Ser/Pro-rich region and a
seven-bladed beta propeller WD40 repeat domain, implicated in protein-protein
interactions. The structure confirms the relationship to the yeast Tup1
corepressor, but reveals important structural differences specific to the
metazoan system. Analysis of missense mutations in the C. elegans Groucho
homolog UNC-37 identifies sites of interaction with repression effectors, and
suggests an induced fit binding site for eh1 domains of Engrailed-type
transcription factors.
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Figure 1.
Figure 1. Domain Structure of Groucho/TLE ProteinsSchematic
diagram of the defined domains in Gro/TLE corepressors.
Glutamine-rich Q domain; glycine/proline-rich GP domain; CcN
domain containing nuclear localization and phosphorylation
sites; serine/threonine-proline-rich SP domain; and WD40 repeat
domain. Residue numbers defining domain boundaries are for human
TLE1. Regions of Groucho/TLE proteins implicated in interaction
with transcription factors are indicated below (horizontal
lines), while those implicated in interactions with repression
effectors are indicated above. In many cases, involvement of a
particular region of Gro/TLE has only been defined by loss of
function on deletion of that region, and not by positive
demonstration of interaction.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
751-761)
copyright 2002.
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