2z6g
From Proteopedia
Crystal Structure of a Full-Length Zebrafish Beta-Catenin
Structural highlights
FunctionCTNB1_DANRE Key downstream component of the canonical Wnt signaling pathway (By similarity). In the absence of Wnt, forms a complex with axin1, axin2, apc, csnk1a1 and gsk3b that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of ctnnb1 and its subsequent degradation by the proteasome (By similarity). In the presence of Wnt ligand, ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (By similarity). Plays a key role in dorsoventral patterning: in prospective ventral blastomeres, its down-regulation by axin1 and axin2 leads to inhibit the Wnt signaling pathway, while in prospective dorsal blastomeres, degradation of axin results in stabilization and nuclear translocation of ctnnb1 (PubMed:8562427, PubMed:30467143).[UniProtKB:P35222][UniProtKB:Q02248][1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedbeta-catenin plays essential roles in cell adhesion and Wnt signaling, while deregulation of beta-catenin is associated with multiple diseases including cancers. Here, we report the crystal structures of full-length zebrafish beta-catenin and a human beta-catenin fragment that contains both the armadillo repeat and the C-terminal domains. Our structures reveal that the N-terminal region of the C-terminal domain, a key component of the C-terminal transactivation domain, forms a long alpha helix that packs on the C-terminal end of the armadillo repeat domain, and thus forms part of the beta-catenin superhelical core. The existence of this helix redefines our view of interactions of beta-catenin with some of its critical partners, including ICAT and Chibby, which may form extensive interactions with this C-terminal domain alpha helix. Our crystallographic and NMR studies also suggest that the unstructured N-terminal and C-terminal tails interact with the ordered armadillo repeat domain in a dynamic and variable manner. Crystal structure of a full-length beta-catenin.,Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W Structure. 2008 Mar;16(3):478-87. PMID:18334222[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Danio rerio | Large Structures | Liu J | Moon R | Takemaru K | Xing Y | Xu W | Zheng J
