6N8S
Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). aPKC phosphorylated, crystal form 3.
Summary for 6N8S
| Entry DOI | 10.2210/pdb6n8s/pdb |
| Descriptor | Lethal(2) giant larvae protein homolog 2 (1 entity in total) |
| Functional Keywords | lgl, polarity, beta propeller, lipid binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 218550.22 |
| Authors | Almagor, L.,Weis, W.I. (deposition date: 2018-11-30, release date: 2019-05-08, Last modification date: 2024-03-13) |
| Primary citation | 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 Cited by 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: 31088962DOI: 10.1073/pnas.1821514116 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.9 Å) |
Structure validation
Download full validation report
