| pmid | 10882138 | ||
|---|---|---|---|
| title | Structure of the dimerization and beta-catenin-binding region of alpha-catenin. | ||
| authors |
|
||
| journal | Mol Cell | ||
| year | 2000 | ||
| full_text_available | false | ||
| doi | 10.1016/s1097-2765(00)80447-5 |
Authors: Pokutta S, Weis WI Journal: Mol Cell (2000) DOI: 10.1016/s1097-2765(00)80447-5
- Mol Cell. 2000 Mar;5(3):533-43. doi: 10.1016/s1097-2765(00)80447-5.
Structure of the dimerization and beta-catenin-binding region of alpha-catenin.
Pokutta S(1), Weis WI.
Author information: (1)Department of Structural Biology, Stanford University School of Medicine, California 94305, USA.
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.
DOI: 10.1016/s1097-2765(00)80447-5 PMID: 10882138 [Indexed for MEDLINE]