1m1e
From Proteopedia
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Beta-catenin armadillo repeat domain bound to ICAT
Overview
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.
About this Structure
1M1E is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 18:06:18 2007
