1DOW

Structure of the dimerization and beta-catenin-binding region of alpha-catenin.

(2000) Mol Cell 5: 533-543

• PubMed: 10882138 Search on PubMed
• DOI: https://doi.org/10.1016/s1097-2765(00)80447-5
• Primary Citation of Related Structures:  
  1DOV, 1DOW


• PubMed Abstract: 
  

  In adherens junctions, alpha-catenin links the cadherin-beta-catenin complex to the actin-based cytoskeleton. alpha-catenin is a homodimer in solution, but forms a 1:1 heterodimer with beta-catenin. The crystal structure of the alpha-catenin dimerization domain, residues 82-279, shows that alpha-catenin dimerizes through formation of a four-helix bundle in which two antiparallel helices are contributed by each protomer. A slightly larger fragment, comprising residues 57-264, binds to beta-catenin. A chimera consisting of the alpha-catenin-binding region of beta-catenin linked to the amino terminus of alpha-catenin 57-264 behaves as a monomer in solution, as expected, since beta-catenin binding disrupts the alpha-catenin dimer. The crystal structure of this chimera reveals the interaction between alpha- and beta-catenin, and provides a basis for understanding adherens junction assembly.

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Organizational Affiliation: 

Department of Structural Biology, Stanford University School of Medicine, California 94305, USA.