This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1dow
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1dow" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dow, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...)
Next diff →
Revision as of 11:20, 20 November 2007
|
CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN
Overview
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 Structure
1DOW is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 13:27:15 2007
