1DK8

CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN

1DK8 の概要

• エントリーDOI: 10.2210/pdb1dk8/pdb
• 関連するPDBエントリー: 1AGR 1CMZ 1EMU
• 分子名称: AXIN, SULFATE ION, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, ... (5 entities in total)
• 機能のキーワード: alpha-helix, pi-helix, signaling protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17985.20

構造登録者

Spink, K.E.,Polakis, P.,Weis, W.I. (登録日: 1999-12-06, 公開日: 2000-07-12, 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

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

実験手法

X-RAY DIFFRACTION (1.57 Å)