1dov

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dov OCA], [http://www.ebi.ac.uk/pdbsum/1dov PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dov RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN'''
'''CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN'''
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[[Category: Pokutta, S.]]
[[Category: Pokutta, S.]]
[[Category: Weis, W I.]]
[[Category: Weis, W I.]]
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[[Category: four-helix bundle]]
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[[Category: Four-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:05:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:45:46 2008''
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Revision as of 11:05, 2 May 2008

Image:1dov.gif

Template:STRUCTURE 1dov

CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN


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

1DOV is a Single protein structure of sequence 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 Fri May 2 14:05:54 2008

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