1MC7

Solution Structure of mDvl1 PDZ domain

1MC7 の概要

• エントリーDOI: 10.2210/pdb1mc7/pdb
• 分子名称: Segment polarity protein dishevelled homolog DVL-1 (1 entity in total)
• 機能のキーワード: pdz domain, wnt signaling, signaling protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P51141
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10204.45

構造登録者

Wong, H.-C.,Bourdelas, A.,Shao, Y.,Wu, D.,Shi, D.L.,Zheng, J. (登録日: 2002-08-05, 公開日: 2003-09-23, 最終更新日: 2024-05-22)

主引用文献

Wong, H.-C.,Bourdelas, A.,Krauss, A.,Lee, H.-J.,Shao, Y.,Wu, D.,Mlodzik, M.,Shi, D.-L.,Zheng, J.
Direct binding of the PDZ domain of Dishevelled to a conserved internal sequence in the C-terminal region of Frizzled
Mol.Cell, 12:1251-1260, 2003

PubMed Abstract: The cytoplasmic protein Dishevelled (Dvl) and the associated membrane-bound receptor Frizzled (Fz) are essential in canonical and noncanonical Wnt signaling pathways. However, the molecular mechanisms underlying this signaling are not well understood. By using NMR spectroscopy, we determined that an internal sequence of Fz binds to the conventional peptide binding site in the PDZ domain of Dvl; this type of site typically binds to C-terminal binding motifs. The C-terminal region of the Dvl inhibitor Dapper (Dpr) and Frodo bound to the same site. In Xenopus, Dvl binding peptides of Fz and Dpr/Frodo inhibited canonical Wnt signaling and blocked Wnt-induced secondary axis formation in a dose-dependent manner, but did not block noncanonical Wnt signaling mediated by the DEP domain. Together, our results identify a missing molecular connection within the Wnt pathway. Differences in the binding affinity of the Dvl PDZ domain and its binding partners may be important in regulating signal transduction by Dvl.

PubMed: 14636582
DOI: 10.1016/S1097-2765(03)00427-1

実験手法

SOLUTION NMR