Armadillo repeat

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Armadillo repeat domain
PDB 3bct EBI.jpg
Structure of the armadillo domain of β-catenin. [1]
Identifiers
SymbolArm
Pfam PF00514
Pfam clan CL0020
InterPro IPR000225
SMART SM00185
PROSITE PS50176
SCOP2 3bct / SCOPe / SUPFAM
CDD cd00020
Membranome 350
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

An armadillo repeat is a characteristic, repetitive amino acid sequence of about 42 residues in length that is found in many proteins. Proteins that contain armadillo repeats typically contain several tandemly repeated copies. [2] [3] Each armadillo repeat is composed of a pair of alpha helices that form a hairpin structure. Multiple copies of the repeat form what is known as an alpha solenoid structure.

Contents

Examples of proteins that contain armadillo repeats include β-catenin, Sarm1 (SARM1), [4] α-importin, [5] plakoglobin, [6] adenomatous polyposis coli (APC), [7] and many others.

The term armadillo derives from the historical name of the β-catenin gene in the fruitfly Drosophila , where the armadillo repeat was first discovered. Although β-catenin was previously believed to be a protein involved in linking cadherin cell adhesion proteins to the cytoskeleton, recent work indicates that β-catenin regulates the homodimerization of alpha-catenin, which in turn controls actin branching and bundling. [8] But, the armadillo repeat is found in a wide range of proteins with other functions. This type of protein domain is important in transducing WNT signals during embryonic development.

Structure

The 3-dimensional fold of an armadillo repeat was first observed in the crystal structure of β-catenin, where the 12 tandem repeats form a superhelix of alpha helices with three helices per unit. [1] The cylindrical structure features a positively charged groove, which presumably interacts with the acidic surfaces of the known interaction partners of β-catenin. [9]

References

  1. 1 2 Huber AH, Nelson WJ, Weis WI (September 1997). "Three-dimensional structure of the armadillo repeat region of β-catenin". Cell. 90 (5): 871–82. doi: 10.1016/S0092-8674(00)80352-9 . PMID   9298899. S2CID   18612343.
  2. ↑ Peifer M, Berg S, Reynolds AB (1994). "A repeating amino acid motif shared by proteins with diverse cellular roles". Cell. 76 (5): 789–91. doi:10.1016/0092-8674(94)90353-0. PMID   7907279. S2CID   26528190.
  3. ↑ Groves MR, Barford D (1999). "Topological characteristics of helical repeat proteins". Current Opinion in Structural Biology. 9 (3): 383–9. doi:10.1016/S0959-440X(99)80052-9. PMID   10361086.
  4. ↑ "Scopus preview - Scopus - Welcome to Scopus". www.scopus.com. Retrieved 2023-03-21.
  5. ↑ Herold A, Truant R, Wiegand H, Cullen BR (October 1998). "Determination of the functional domain organization of the importin alpha nuclear import factor". J. Cell Biol. 143 (2): 309–18. doi:10.1083/jcb.143.2.309. PMC   2132842 . PMID   9786944.
  6. ↑ McCrea PD, Turck CW, Gumbiner B (November 1991). "A homolog of the armadillo protein in Drosophila (plakoglobin) associated with E-cadherin". Science. 254 (5036): 1359–61. Bibcode:1991Sci...254.1359M. doi:10.1126/science.1962194. PMID   1962194.
  7. ↑ Hirschl D, Bayer P, Müller O (March 1996). "Secondary structure of an armadillo single repeat from the APC protein". FEBS Lett. 383 (1–2): 31–6. doi:10.1016/0014-5793(96)00215-3. PMID   8612785. S2CID   36190869.
  8. ↑ Nusse, Roel, and Hans Clevers. “Wnt/β-Catenin Signaling, Disease, and Emerging Therapeutic Modalities.” Cell, vol. 169, no. 6, 1 June 2017, pp. 985–999., doi:10.1016/j.cell.2017.05.016.
  9. ↑ "Armadillo (IPR000225)". InterPro. EMBL-EBI.


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