1dov
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CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN
OverviewOverview
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.
About this StructureAbout this Structure
1DOV is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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
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