2Z6H

Crystal Structure of Beta-Catenin Armadillo Repeat Region and Its C-Terminal domain

Summary for 2Z6H

• Entry DOI: 10.2210/pdb2z6h/pdb
• Related: 2Z6G
• Descriptor: Catenin beta-1 (2 entities in total)
• Functional Keywords: beta-catenin, c-terminal domain, activator, alternative splicing, cell adhesion, cytoplasm, cytoskeleton, disease mutation, nucleus, phosphorylation, polymorphism, structural protein, transcription, transcription regulation, ubl conjugation, wnt signaling pathway
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P35222
• Total number of polymer chains: 1
• Total formula weight: 70417.73

Authors

Xing, Y.,Takemaru, K.,Liu, J.,Zheng, J.,Moon, R.,Xu, W. (deposition date: 2007-08-01, release date: 2008-02-12, Last modification date: 2024-03-13)

Primary citation

Xing, Y.,Takemaru, K.,Liu, J.,Berndt, J.D.,Zheng, J.J.,Moon, R.T.,Xu, W.
Crystal Structure of a Full-Length beta-Catenin
Structure, 16:478-487, 2008

PubMed Abstract: beta-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.

PubMed: 18334222
DOI: 10.1016/j.str.2007.12.021

Experimental method

X-RAY DIFFRACTION (2.2 Å)