{PDOC50176}
{PS50176; ARM_REPEAT}
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* Armadillo/plakoglobin ARM repeat profile *
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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 beta-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  beta-catenin  [4].  There,  the  12 repeats form a superhelix of
alpha-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 beta-catenin.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: 3.
-Last update: December 2001 / First entry.

[ 1] Peifer M., Berg S., Reynolds A.B.
     "A repeating amino acid motif shared by proteins with diverse cellular
     roles."
     Cell 76:789-791(1994).
     PubMed=7907279
[ 2] Groves M.R., Barford D.
     "Topological characteristics of helical repeat proteins."
     Curr. Opin. Struct. Biol. 9:383-389(1999).
     PubMed=10361086
[ 3] Hatzfeld M.
     "The armadillo family of structural proteins."
     Int. Rev. Cytol. 186:179-224(1999).
     PubMed=9770300
[ 4] Huber A.H., Nelson W.J., Weis W.I.
     "Three-dimensional structure of the armadillo repeat region of
     beta-catenin."
     Cell 90:871-882(1997).
     PubMed=9298899

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