3c2h | pdb_00003c2h

Crystal Structure of SYS-1 at 2.6A resolution

spinqualitylabelsall models 3c2h, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3c2h is a 2 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: FLC, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9XVI2_CAEEL Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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