1dow
From Proteopedia
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- | [[Image:1dow.gif|left|200px]] | + | [[Image:1dow.gif|left|200px]] |
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- | '''CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN''' | + | {{Structure |
+ | |PDB= 1dow |SIZE=350|CAPTION= <scene name='initialview01'>1dow</scene>, resolution 1.80Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1DOW is a [ | + | 1DOW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10882138 10882138] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:41:53 2008'' |
Revision as of 08:41, 20 March 2008
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, resolution 1.80Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
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 Thu Mar 20 10:41:53 2008