2Z6G

Crystal Structure of a Full-Length Zebrafish Beta-Catenin

2Z6G の概要

• エントリーDOI: 10.2210/pdb2z6g/pdb
• 関連するPDBエントリー: 2Z6H
• 分子名称: B-catenin (1 entity in total)
• 機能のキーワード: full-length, beta-catenin, cell adhesion
• 由来する生物種: Danio rerio (zebrafish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 85634.34

構造登録者

Xing, Y.,Takemaru, K.,Liu, J.,Zheng, J.,Moon, R.,Xu, W. (登録日: 2007-08-01, 公開日: 2008-02-12, 最終更新日: 2023-11-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.4 Å)