2BCT
THE ARMADILLO REPEAT REGION FROM MURINE BETA-CATENIN
Summary for 2BCT
Entry DOI | 10.2210/pdb2bct/pdb |
Descriptor | BETA-CATENIN (1 entity in total) |
Functional Keywords | armadillo repeat, beta-catenin, structural protein |
Biological source | Mus musculus (house mouse) |
Cellular location | Cytoplasm: Q02248 |
Total number of polymer chains | 1 |
Total formula weight | 56314.34 |
Authors | Huber, A.H.,Nelson, W.J.,Weis, W.I. (deposition date: 1997-07-30, release date: 1997-10-15, Last modification date: 2024-05-22) |
Primary citation | Huber, A.H.,Nelson, W.J.,Weis, W.I. Three-dimensional structure of the armadillo repeat region of beta-catenin. Cell(Cambridge,Mass.), 90:871-882, 1997 Cited by PubMed Abstract: 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. PubMed: 9298899DOI: 10.1016/S0092-8674(00)80352-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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