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4UZ7

STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM VI - 2.2A

4UZ7 の概要
エントリーDOI10.2210/pdb4uz7/pdb
関連するPDBエントリー4UYU 4UYW 4UYZ 4UZ1 4UZ5 4UZ6 4UZ9 4UZA 4UZJ 4UZK 4UZL 4UZQ
分子名称PROTEIN NOTUM HOMOLOG, CHLORIDE ION (3 entities in total)
機能のキーワードhydrolase, wnt, esterase, extracellular, alpha/beta hydrolase
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Secreted : Q6P988
タンパク質・核酸の鎖数2
化学式量合計87169.75
構造登録者
Zebisch, M.,Jones, E.Y. (登録日: 2014-09-04, 公開日: 2015-02-25, 最終更新日: 2015-03-18)
主引用文献Kakugawa, S.,Langton, P.F.,Zebisch, M.,Howell, S.A.,Chang, T.,Liu, Y.,Feizi, T.,Bineva, G.,O'Reilly, N.,Snijders, A.P.,Jones, E.Y.,Vincent, J.
Notum Deacylates Wnt Proteins to Suppress Signalling Activity.
Nature, 519:187-, 2015
Cited by
PubMed Abstract: Signalling by Wnt proteins is finely balanced to ensure normal development and tissue homeostasis while avoiding diseases such as cancer. This is achieved in part by Notum, a highly conserved secreted feedback antagonist. Notum has been thought to act as a phospholipase, shedding glypicans and associated Wnt proteins from the cell surface. However, this view fails to explain specificity, as glypicans bind many extracellular ligands. Here we provide genetic evidence in Drosophila that Notum requires glypicans to suppress Wnt signalling, but does not cleave their glycophosphatidylinositol anchor. Structural analyses reveal glycosaminoglycan binding sites on Notum, which probably help Notum to co-localize with Wnt proteins. They also identify, at the active site of human and Drosophila Notum, a large hydrophobic pocket that accommodates palmitoleate. Kinetic and mass spectrometric analyses of human proteins show that Notum is a carboxylesterase that removes an essential palmitoleate moiety from Wnt proteins and thus constitutes the first known extracellular protein deacylase.
PubMed: 25731175
DOI: 10.1038/NATURE14259
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 4uz7
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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