5y3c

Crystal structure of zebrafish Ccd1 DIX domain

spinqualitylabelsall models 5y3c, resolution 1.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5y3c is a 1 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.96Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DIX1A_DANRE Publication Abstract from PubMed Wnt signaling plays an important role in governing cell fate decisions. Coiled-coil-DIX1 (Ccd1), Dishevelled (Dvl), and Axin are signaling proteins that regulate the canonical pathway by controlling the stability of a key signal transducer beta-catenin. These proteins contain the DIX domain with a ubiquitin-like fold, which mediates their interaction in the beta-catenin destruction complex through dynamic head-to-tail polymerization. Despite high sequence similarities, mammalian Ccd1 shows weaker stimulation of beta-catenin transcriptional activity compared with zebrafish (z) Ccd1 in cultured cells. Here, we show that the mouse (m) Ccd1 DIX domain displays weaker ability for homopolymerization than that of zCcd1. Furthermore, X-ray crystallographic analysis of mCcd1 and zCcd1 DIX domains revealed that mCcd1 was assembled into a double-helical filament by the insertion of the beta1-beta2 loop into the head-to-tail interface, whereas zCcd1 formed a typical single-helical polymer similar to Dvl1 and Axin. The mutation in the contact interface of mCcd1 double-helical polymer changed the hydrodynamic properties of mCcd1 so that it acquired the ability to induce Wnt-specific transcriptional activity similar to zCcd1. These findings suggest a novel regulatory mechanism by which mCcd1 modulates Wnt signaling through auto-inhibition of dynamic head-to-tail homopolymerization. Structural basis for Ccd1 auto-inhibition in the Wnt pathway through homomerization of the DIX domain.,Terawaki SI, Fujita S, Katsutani T, Shiomi K, Keino-Masu K, Masu M, Wakamatsu K, Shibata N, Higuchi Y Sci Rep. 2017 Aug 10;7(1):7739. doi: 10.1038/s41598-017-08019-5. PMID:28798413 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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