Your browser version may not work well with NCBI's Web applications. More information here...
1: Cell. 1997 Sep 5;90(5):871-82.Click here to read Links

Three-dimensional structure of the armadillo repeat region of beta-catenin.

Huber AH, Nelson WJ, Weis WI.

Department of Structural Biology, Stanford University School of Medicine, California 94305, USA.

Beta-catenin is essential for cadherin-based cell adhesion and Wnt/Wingless growth factor signaling. In these roles, it binds to cadherins, Tcf-family transcription factors, and the tumor suppressor gene product Adenomatous Polyposis Coli (APC). A core region of beta-catenin, composed of 12 copies of a 42 amino acid sequence motif known as an armadillo repeat, mediates these interactions. The three-dimensional structure of a protease-resistant fragment of beta-catenin containing the armadillo repeat region has been determined. The 12 repeats form a superhelix of helices that features a long, positively charged groove. Although unrelated in sequence, the beta-catenin binding regions of cadherins, Tcfs, and APC are acidic and are proposed to interact with this groove.

PMID: 9298899 [PubMed - indexed for MEDLINE]

Structures reported by this article