6N8P

Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). Unphosphorylated, crystal form 1.

6N8P の概要

• エントリーDOI: 10.2210/pdb6n8p/pdb
• 分子名称: Lethal(2) giant larvae protein homolog 2, CHLORIDE ION (2 entities in total)
• 機能のキーワード: lgl, polarity, beta propeller, lipid binding 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: 109310.56

構造登録者

Almagor, L.,Weis, W.I. (登録日: 2018-11-30, 公開日: 2019-05-08, 最終更新日: 2024-03-13)

主引用文献

Almagor, L.,Ufimtsev, I.S.,Ayer, A.,Li, J.,Weis, W.I.
Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2.
Proc.Natl.Acad.Sci.USA, 116:10804-10812, 2019

PubMed Abstract: Metazoan cell polarity is controlled by a set of highly conserved proteins. Lethal giant larvae (Lgl) functions in apical-basal polarity through phosphorylation-dependent interactions with several other proteins as well as the plasma membrane. Phosphorylation of Lgl by atypical protein kinase C (aPKC), a component of the partitioning-defective (Par) complex in epithelial cells, excludes Lgl from the apical membrane, a crucial step in the establishment of epithelial cell polarity. We present the crystal structures of human Lgl2 in both its unphosphorylated and aPKC-phosphorylated states. Lgl2 adopts a double β-propeller structure that is unchanged by aPKC phosphorylation of an unstructured loop in its second β-propeller, ruling out models of phosphorylation-dependent conformational change. We demonstrate that phosphorylation controls the direct binding of purified Lgl2 to negative phospholipids in vitro. We also show that a coil-helix transition of this region that is promoted by phosphatidylinositol 4,5-bisphosphate (PIP) is also phosphorylation-dependent, implying a highly effective phosphorylative switch for membrane association.

PubMed: 31088962
DOI: 10.1073/pnas.1821514116

実験手法

X-RAY DIFFRACTION (3.193 Å)