1DOW

CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN

Summary for 1DOW

• Entry DOI: 10.2210/pdb1dow/pdb
• Descriptor: ALPHA-CATENIN, BETA-CATENIN (3 entities in total)
• Functional Keywords: four-helix bundle, cell adhesion
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 26361.34

Authors

Pokutta, S.,Weis, W.I. (deposition date: 1999-12-21, release date: 2000-07-12, Last modification date: 2024-11-13)

Primary citation

Pokutta, S.,Weis, W.I.
Structure of the dimerization and beta-catenin-binding region of alpha-catenin.
Mol.Cell, 5:533-543, 2000

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.

PubMed: 10882138
DOI: 10.1016/S1097-2765(00)80447-5

Experimental method

X-RAY DIFFRACTION (1.8 Å)