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Armadillo repeat

April 16, 2024

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.

Armadillo repeat domain
Structure of the armadillo domain of β-catenin.[1]
Identifiers
SymbolArm
PfamPF00514
Pfam clanCL0020
InterProIPR000225
SMARTSM00185
PROSITEPS50176
SCOP23bct / SCOPe / SUPFAM
CDDcd00020
Membranome350
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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 edit

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 edit

  1. ^ a b 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.

External links edit


 

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April 16, 2024
armadillo, repeat, armadillo, repeat, characteristic, repetitive, amino, acid, sequence, about, residues, length, that, found, many, proteins, proteins, that, contain, armadillo, repeats, typically, contain, several, tandemly, repeated, copies, each, armadillo. 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 Armadillo repeat domainStructure of the armadillo domain of b catenin 1 IdentifiersSymbolArmPfamPF00514Pfam clanCL0020InterProIPR000225SMARTSM00185PROSITEPS50176SCOP23bct SCOPe SUPFAMCDDcd00020Membranome350Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryExamples of proteins that contain armadillo repeats include b catenin Sarm1 SARM1 4 a importin 5 plakoglobin 6 adenomatous polyposis coli APC 7 and many others The term armadillo derives from the historical name of the b catenin gene in the fruitfly Drosophila where the armadillo repeat was first discovered Although b catenin was previously believed to be a protein involved in linking cadherin cell adhesion proteins to the cytoskeleton recent work indicates that b 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 editThe 3 dimensional fold of an armadillo repeat was first observed in the crystal structure of b 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 b catenin 9 References edit a b Huber AH Nelson WJ Weis WI September 1997 Three dimensional structure of the armadillo repeat region of b catenin Cell 90 5 871 82 doi 10 1016 S0092 8674 00 80352 9 PMID 9298899 S2CID 18612343 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 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 Scopus preview Scopus Welcome to Scopus www scopus com Retrieved 2023 03 21 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 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 Hirschl D Bayer P Muller 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 Nusse Roel and Hans Clevers Wnt I 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 Armadillo IPR000225 InterPro EMBL EBI External links editEukaryotic Linear Motif resource motif class TRG NLS Bipartite 1 Eukaryotic Linear Motif resource motif class TRG NLS MonoCore 2 Eukaryotic Linear Motif resource motif class TRG NLS MonoExtC 3 Eukaryotic Linear Motif resource motif class TRG NLS MonoExtN 4 Armadillo Domain Proteins at the U S National Library of Medicine Medical Subject Headings MeSH Armadillo plakoglobin ARM repeat permanent dead link in PROSITE nbsp This molecular biology article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Armadillo repeat amp oldid 1188005824, wikipedia, wiki, book, books, library,

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