1dov
From Proteopedia
(New page: 200px<br /><applet load="1dov" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dov, resolution 3.00Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1dov.gif|left|200px]]<br /><applet load="1dov" size=" | + | [[Image:1dov.gif|left|200px]]<br /><applet load="1dov" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dov, resolution 3.00Å" /> | caption="1dov, resolution 3.00Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN'''<br /> | '''CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In adherens junctions, alpha-catenin links the cadherin-beta-catenin | + | 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== | ||
| - | 1DOV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1DOV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1DOV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Pokutta, S.]] | [[Category: Pokutta, S.]] | ||
| - | [[Category: Weis, W | + | [[Category: Weis, W I.]] |
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:51 2008'' |
Revision as of 10:18, 21 February 2008
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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 Thu Feb 21 12:18:51 2008
