1JPP

The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin

1JPP の概要

• エントリーDOI: 10.2210/pdb1jpp/pdb
• 分子名称: BETA-CATENIN, ADENOMATOUS POLYPOSIS COLI PROTEIN, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: disease mutation, anti-oncogene, cell adhesion
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Cytoplasm: Q02248; Cell junction, adherens junction: P25054
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 121354.15

構造登録者

Spink, K.E.,Fridman, S.G.,Weis, W.I. (登録日: 2001-08-02, 公開日: 2002-01-16, 最終更新日: 2023-08-16)

主引用文献

Eklof Spink, K.,Fridman, S.G.,Weis, W.I.
Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex.
EMBO J., 20:6203-6212, 2001

PubMed Abstract: The adenomatous polyposis coli (APC) tumor suppressor protein plays a critical role in regulating cellular levels of the oncogene product beta-catenin. APC binds to beta-catenin through a series of homologous 15 and 20 amino acid repeats. We have determined the crystal structure of a 15 amino acid beta-catenin binding repeat from APC bound to the armadillo repeat region of beta-catenin. Although it lacks significant sequence homology, the N-terminal half of the repeat binds in a manner similar to portions of E-cadherin and XTcf3, but the remaining interactions are unique to APC. We discuss the implications of this new structure for the design of therapeutics, and present evidence from structural, biochemical and sequence data, which suggest that the 20 amino acid repeats can adopt two modes of binding to beta-catenin.

PubMed: 11707392
DOI: 10.1093/emboj/20.22.6203

実験手法

X-RAY DIFFRACTION (3.1 Å)