1M1E

Beta-catenin armadillo repeat domain bound to ICAT

Summary for 1M1E

• Entry DOI: 10.2210/pdb1m1e/pdb
• Descriptor: Beta-catenin, ICAT (3 entities in total)
• Functional Keywords: cell adhesion, cytoskeleton, armadillo repeats, transciption factor, structural protein
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cytoplasm: Q02248; Cytoplasm (By similarity): Q9NSA3
• Total number of polymer chains: 2
• Total formula weight: 68025.46

Authors

Daniels, D.L.,Weis, W.I. (deposition date: 2002-06-18, release date: 2002-10-16, Last modification date: 2024-02-14)

Primary citation

Daniels, D.L.,Weis, W.I.
ICAT inhibits Beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules.
Mol.Cell, 10:573-584, 2002

PubMed Abstract: 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.

PubMed: 12408825
DOI: 10.1016/S1097-2765(02)00631-7

Experimental method

X-RAY DIFFRACTION (2.1 Å)