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|1dow, resolution 1.80Å ()|
CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN
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.
Structure of the dimerization and beta-catenin-binding region of alpha-catenin., Pokutta S, Weis WI, Mol Cell. 2000 Mar;5(3):533-43. PMID:10882138
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Pokutta S, Weis WI. Structure of the dimerization and beta-catenin-binding region of alpha-catenin. Mol Cell. 2000 Mar;5(3):533-43. PMID:10882138