1DOV
CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN
Summary for 1DOV
| Entry DOI | 10.2210/pdb1dov/pdb |
| Descriptor | ALPHA-CATENIN (1 entity in total) |
| Functional Keywords | four-helix bundle, cell adhesion |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 19875.95 |
| Authors | Pokutta, S.,Weis, W.I. (deposition date: 1999-12-21, release date: 2000-07-12, Last modification date: 2024-02-07) |
| 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 Cited by 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: 10882138DOI: 10.1016/S1097-2765(00)80447-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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