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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q9XVI2_CAEEL Q9XVI2_CAEEL] | | [https://www.uniprot.org/uniprot/Q9XVI2_CAEEL Q9XVI2_CAEEL] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| C. elegans SYS-1 has key functional characteristics of a canonical beta-catenin, but no significant sequence similarity. Here, we report the SYS-1 crystal structure, both on its own and in a complex with POP-1, the C. elegans TCF homolog. The two structures possess signature features of canonical beta-catenin and the beta-catenin/TCF complex that could not be predicted by sequence. Most importantly, SYS-1 bears 12 armadillo repeats and the SYS-1/POP-1 interface is anchored by a conserved salt-bridge, the "charged button." We also modeled structures for three other C. elegans beta-catenins to predict the molecular basis of their distinct binding properties. Finally, we generated a phylogenetic tree, using the region of highest structural similarity between SYS-1 and beta-catenin, and found that SYS-1 clusters robustly within the beta-catenin clade. We conclude that the SYS-1 protein belongs to the beta-catenin family and suggest that additional divergent beta-catenins await discovery.
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| The C. elegans SYS-1 protein is a bona fide beta-catenin.,Liu J, Phillips BT, Amaya MF, Kimble J, Xu W Dev Cell. 2008 May;14(5):751-61. PMID:18477457<ref>PMID:18477457</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3c2h" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
