Armadillo repeat

Armadillo repeat domain

Structure of the armadillo domain of beta-catenin.[1]
Identifiers
Symbol Arm
Pfam PF00514
Pfam clan CL0020
InterPro IPR000225
SMART SM00185
PROSITE PS50176
SCOP 3bct
SUPERFAMILY 3bct
CDD cd00020

An armadillo repeat is the name of a characteristic, repetitive amino acid sequence of about 40 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.

Examples of proteins that contain armadillo repeats include β-catenin, α-importin,[4] plakoglobin,[5] adenomatous polyposis coli (APC),[6] 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. β-catenin is a protein involved in linking cadherin cell adhesion proteins to the cytoskeleton,[1] 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 beta-catenin, where the 12 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 beta-catenin.[7]

References

  1. 1 2 3 Huber AH, Nelson WJ, Weis WI (September 1997). "Three-dimensional structure of the armadillo repeat region of beta-catenin". Cell 90 (5): 871–82. doi:10.1016/S0092-8674(00)80352-9. PMID 9298899.
  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.
  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. 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.
  5. 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. doi:10.1126/science.1962194. PMID 1962194.
  6. 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.
  7. "Armadillo (IPR000225)". InterPro. EMBL-EBI.

External links


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