PROSITE documentation PDOC50176Armadillo/plakoglobin ARM repeat profile
The armadillo repeat is an approximately 40 amino acids long tandemly repeated sequence motif first identified in the Drosophila segment polarity gene product armadillo, a protein that mediates cell adhesion. Similar repeats were later found in the mammalian armadillo homolog β-catenin, the junctional plaque protein plakoglobin, the adenomatous polyposis coli (APC) tumor suppressor protein, and a number of other proteins [1]. These proteins exert several functions through interactions of their tandem armadillo repeats domain with diverse binding partners. The proteins combine structural roles as cell-contact and cytoskeleton-associated proteins and signaling functions by generating and transducing signals affecting gene expression [1,2,3].
The three-dimensional fold of an armadillo repeat is known from the crystal structure of β-catenin [4]. There, the 12 repeats form a superhelix of α-helices, with three helices per unit. The cylindrical structure features a positively charged grove which presumably interacts with the acidic surfaces of the known interaction partners of β-catenin.
Last update:December 2001 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Peifer M. Berg S. Reynolds A.B. |
Title | A repeating amino acid motif shared by proteins with diverse cellular roles. | |
Source | Cell 76:789-791(1994). | |
PubMed ID | 7907279 |
2 | Authors | Groves M.R. Barford D. |
Title | Topological characteristics of helical repeat proteins. | |
Source | Curr. Opin. Struct. Biol. 9:383-389(1999). | |
PubMed ID | 10361086 |
3 | Authors | Hatzfeld M. |
Title | The armadillo family of structural proteins. | |
Source | Int. Rev. Cytol. 186:179-224(1999). | |
PubMed ID | 9770300 |
4 | Authors | Huber A.H. Nelson W.J. Weis W.I. |
Title | Three-dimensional structure of the armadillo repeat region of beta-catenin. | |
Source | Cell 90:871-882(1997). | |
PubMed ID | 9298899 |
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