6IW3

High resolution structure of Dvl2-DIX Y27W/C80S mutant

6IW3 の概要

• エントリーDOI: 10.2210/pdb6iw3/pdb
• 分子名称: Segment polarity protein dishevelled homolog DVL-2 (2 entities in total)
• 機能のキーワード: wnt signalling, 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: 9311.48

構造登録者

Yamanishi, K.,Shibata, N. (登録日: 2018-12-04, 公開日: 2019-02-20, 最終更新日: 2023-11-22)

主引用文献

Yamanishi, K.,Sin, Y.,Terawaki, S.I.,Higuchi, Y.,Shibata, N.
High-resolution structure of a Y27W mutant of the Dishevelled2 DIX domain.
Acta Crystallogr F Struct Biol Commun, 75:116-122, 2019

PubMed Abstract: Dishevelled (Dvl) is a positive regulator of the canonical Wnt pathway that downregulates the phosphorylation of β-catenin and its subsequent degradation. Dvl contains an N-terminal DIX domain, which is involved in its homooligomerization and interactions with regulators of the Wnt pathway. The crystal structure of a Y27W mutant of the Dishevelled2 DIX domain (DIX-Y27W) has been determined at 1.64 Å resolution. DIX-Y27W has a compact ubiquitin-like fold and self-associates with neighbouring molecules through β-bridges, resulting in a head-to-tail helical molecular arrangement similar to previously reported structures of DIX domains. Glu23 of DIX-Y27W forms a hydrogen bond to the side chain of Trp27, corresponding to the Glu762...Trp766 hydrogen bond of the rat Axin DIX domain, whereas Glu23 in the Y27D mutant of the Dishevelled2 DIX domain forms a salt bridge to Lys68 of the adjacent molecule. The high-resolution DIX-Y27W structure provides details of the head-to-tail interaction, including solvent molecules, and also the plausibly wild-type-like structure of the self-association surface compared with previously published Dvl DIX-domain mutants.

PubMed: 30713163
DOI: 10.1107/S2053230X18018290

実験手法

X-RAY DIFFRACTION (1.64 Å)