1FSH

STRUCTURAL BASIS OF THE RECOGNITION OF THE DISHEVELLED DEP DOMAIN IN THE WNT SIGNALING PATHWAY

1FSH の概要

• エントリーDOI: 10.2210/pdb1fsh/pdb
• 分子名称: DISHEVELLED-1 (1 entity in total)
• 機能のキーワード: three-helix bundle, beta-arm, dishevelled-1, segment polarity protein dishevelled homolog dvl-1, signaling protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11934.70

構造登録者

Wong, H.C.,Zheng, J. (登録日: 2000-09-08, 公開日: 2001-03-08, 最終更新日: 2024-05-29)

主引用文献

Wong, H.C.,Mao, J.,Nguyen, J.T.,Srinivas, S.,Zhang, W.,Liu, B.,Li, L.,Wu, D.,Zheng, J.
Structural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway.
Nat.Struct.Biol., 7:1178-1184, 2000

PubMed Abstract: The DEP domain of Dishevelled (Dvl) proteins transduces signals to effector proteins downstream of Dvl in the Wnt pathway. Here we report that DEP-containing mutants inhibit Wnt-induced, but not Dvl-induced, activation of the transcription factor Lef-1. This inhibitory effect is weakened by a K434M mutation. Nuclear magnetic resonance spectroscopy revealed that the DEP domain of mouse Dvl1 comprises a three-helix bundle, a beta-hairpin 'arm' and two short beta-strands at the C-terminal region. Lys 434 is located at the tip of the beta-hairpin 'arm'. Based on our findings, we conclude that DEP interacts with regulators upstream of Dvl via a strong electric dipole on the molecule's surface created by Lys 434, Asp 445 and Asp 448; the electric dipole and the putative membrane binding site are at two different locations.

PubMed: 11101902
DOI: 10.1038/82047

実験手法

SOLUTION NMR