1m1e: Difference between revisions

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{{STRUCTURE_1m1e|  PDB=1m1e  |  SCENE=  }}  
{{STRUCTURE_1m1e|  PDB=1m1e  |  SCENE=  }}  


'''Beta-catenin armadillo repeat domain bound to ICAT'''
===Beta-catenin armadillo repeat domain bound to ICAT===




==Overview==
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In the canonical Wnt signaling pathway, beta-catenin activates target genes through its interactions with Tcf/Lef-family transcription factors and additional transcriptional coactivators. The crystal structure of ICAT, an inhibitor of beta-catenin-mediated transcription, bound to the armadillo repeat domain of beta-catenin, has been determined. ICAT contains an N-terminal helilical domain that binds to repeats 11 and 12 of beta-catenin, and an extended C-terminal region that binds to repeats 5-10 in a manner similar to that of Tcfs and other beta-catenin ligands. Full-length ICAT dissociates complexes of beta-catenin, Lef-1, and the transcriptional coactivator p300, whereas the helical domain alone selectively blocks binding to p300. The C-terminal armadillo repeats of beta-catenin may be an attractive target for compounds designed to disrupt aberrant beta-catenin-mediated transcription associated with various cancers.
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==About this Structure==
==About this Structure==
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[[Category: Cytoskeleton]]
[[Category: Cytoskeleton]]
[[Category: Transciption factor]]
[[Category: Transciption factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:00:37 2008''

Revision as of 23:00, 2 July 2008

File:1m1e.png

Template:STRUCTURE 1m1e

Beta-catenin armadillo repeat domain bound to ICATBeta-catenin armadillo repeat domain bound to ICAT

Template:ABSTRACT PUBMED 12408825

About this StructureAbout this Structure

1M1E is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules., Daniels DL, Weis WI, Mol Cell. 2002 Sep;10(3):573-84. PMID:12408825

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