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| [[Image:1dow.gif|left|200px]] | | {{Seed}} |
| | [[Image:1dow.png|left|200px]] |
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| {{STRUCTURE_1dow| PDB=1dow | SCENE= }} | | {{STRUCTURE_1dow| PDB=1dow | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN'''
| | ===CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10882138}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10882138 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10882138}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Weis, W I.]] | | [[Category: Weis, W I.]] |
| [[Category: Four-helix bundle]] | | [[Category: Four-helix bundle]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:05:55 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:23:47 2008'' |