| First Author | Pokutta S | Year | 2000 |
| Journal | Mol Cell | Volume | 5 |
| Issue | 3 | Pages | 533-43 |
| PubMed ID | 10882138 | Mgi Jnum | J:61504 |
| Mgi Id | MGI:1355058 | Doi | 10.1016/s1097-2765(00)80447-5 |
| Citation | Pokutta S, et al. (2000) Structure of the dimerization and beta-catenin-binding region of alpha-catenin. Mol Cell 5(3):533-43 |
| abstractText | 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. |
