1O9U

GLYCOGEN SYNTHASE KINASE 3 BETA COMPLEXED WITH AXIN PEPTIDE

1O9U の概要

• エントリーDOI: 10.2210/pdb1o9u/pdb
• 関連するPDBエントリー: 1DK8 1EMU 1GNG 1H8F 1I09 1O6K 1O6L
• 分子名称: GLYCOGEN SYNTHASE KINASE-3 BETA, AXIN PEPTIDE, 9-METHYL-9H-PURIN-6-AMINE, ... (4 entities in total)
• 機能のキーワード: transferase-transferase substrate complex, kinase, insulin pathway, transferase, serine/threonine-protein kinase, atp-binding, multigene family, phosphorylation, developmental protein, anti-oncogene, apoptosis, transferase- transferase substrate complex, transferase/transferase substrate
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41911.06

構造登録者

Dajani, R.,Pearl, L.H.,Roe, S.M. (登録日: 2002-12-19, 公開日: 2003-08-15, 最終更新日: 2024-11-06)

主引用文献

Dajani, R.,Fraser, E.,Roe, S.M.,Yeo, M.,Good, V.,Thompson, V.,Dale, T.C.,Pearl, L.H.
Structural Basis for Recruitment of Glycogen Synthase Kinase 3Beta to the Axin-Apc Scaffold Complex
Embo J., 22:494-, 2003

PubMed Abstract: Glycogen synthase kinase 3beta (GSK3beta) is a serine/threonine kinase involved in insulin, growth factor and Wnt signalling. In Wnt signalling, GSK3beta is recruited to a multiprotein complex via interaction with axin, where it hyperphosphorylates beta-catenin, marking it for ubiquitylation and destruction. We have now determined the crystal structure of GSK3beta in complex with a minimal GSK3beta-binding segment of axin, at 2.4 A resolution. The structure confirms the co-localization of the binding sites for axin and FRAT in the C-terminal domain of GSK3beta, but reveals significant differences in the interactions made by axin and FRAT, mediated by conformational plasticity of the 285-299 loop in GSK3beta. Detailed comparison of the axin and FRAT GSK3beta complexes allows the generation of highly specific mutations, which abrogate binding of one or the other. Quantitative analysis suggests that the interaction of GSK3beta with the axin scaffold enhances phosphorylation of beta-catenin by >20 000-fold.

PubMed: 12554650
DOI: 10.1093/EMBOJ/CDG068

実験手法

X-RAY DIFFRACTION (2.4 Å)