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New page: left|200px<br /><applet load="1dow" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dow, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1dow.gif|left|200px]]<br /><applet load="1dow" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dow.gif|left|200px]]<br /><applet load="1dow" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dow, resolution 1.80&Aring;" />
caption="1dow, resolution 1.80&Aring;" />
'''CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN'''<br />
'''CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN'''<br />


==Overview==
==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.
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==
==About this Structure==
1DOW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DOW OCA].  
1DOW is a [http://en.wikipedia.org/wiki/Protein_complex 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==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Pokutta, S.]]
[[Category: Pokutta, S.]]
[[Category: Weis, W.I.]]
[[Category: Weis, W I.]]
[[Category: four-helix bundle]]
[[Category: four-helix bundle]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:27:15 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:53 2008''