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1EMU

STRUCTURE OF THE AXIN RGS-HOMOLOGOUS DOMAIN IN COMPLEX WITH A SAMP REPEAT FROM APC

1EMU の概要
エントリーDOI10.2210/pdb1emu/pdb
関連するPDBエントリー1DK8
分子名称AXIN, ADENOMATOUS POLYPOSIS COLI PROTEIN, GLYCEROL, ... (4 entities in total)
機能のキーワードrgs domain, signaling protein
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Cytoplasm : O15169
Cell junction, adherens junction : P25054
タンパク質・核酸の鎖数2
化学式量合計17761.17
構造登録者
Spink, K.E.,Polakis, P.,Weis, W.I. (登録日: 2000-03-17, 公開日: 2000-07-05, 最終更新日: 2024-02-07)
主引用文献Spink, K.E.,Polakis, P.,Weis, W.I.
Structural basis of the Axin-adenomatous polyposis coli interaction.
EMBO J., 19:2270-2279, 2000
Cited by
PubMed Abstract: Axin and the adenomatous polyposis coli (APC) tumor suppressor protein are components of the Wnt/Wingless growth factor signaling pathway. In the absence of Wnt signal, Axin and APC regulate cytoplasmic levels of the proto-oncogene beta-catenin through the formation of a large complex containing these three proteins, glycogen synthase kinase 3beta (GSK3beta) and several other proteins. Both Axin and APC are known to be critical for beta-catenin regulation, and truncations in APC that eliminate the Axin-binding site result in human cancers. A protease-resistant domain of Axin that contains the APC-binding site is a member of the regulators of G-protein signaling (RGS) superfamily. The crystal structures of this domain alone and in complex with an Axin-binding sequence from APC reveal that the Axin-APC interaction occurs at a conserved groove on a face of the protein that is distinct from the G-protein interface of classical RGS proteins. The molecular interactions observed in the Axin-APC complex provide a rationale for the evolutionary conservation seen in both proteins.
PubMed: 10811618
DOI: 10.1093/emboj/19.10.2270
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 1emu
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-30に公開中

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