7KC4
Human WLS in complex with WNT8A
Summary for 7KC4
| Entry DOI | 10.2210/pdb7kc4/pdb |
| EMDB information | 22806 |
| Descriptor | Protein Wnt-8a, Protein wntless homolog, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | g-protein coupled receptor, palmitoleation, secretion, embryonic development, membrane protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 110183.28 |
| Authors | Nygaard, R.,Jia, Y.,Kim, J.,Ross, D.,Parisi, G.,Clarke, O.B.,Virshup, D.M.,Mancia, F. (deposition date: 2020-10-05, release date: 2021-01-06, Last modification date: 2024-10-09) |
| Primary citation | Nygaard, R.,Yu, J.,Kim, J.,Ross, D.R.,Parisi, G.,Clarke, O.B.,Virshup, D.M.,Mancia, F. Structural Basis of WLS/Evi-Mediated Wnt Transport and Secretion. Cell, 184:194-, 2021 Cited by PubMed Abstract: Wnts are evolutionarily conserved ligands that signal at short range to regulate morphogenesis, cell fate, and stem cell renewal. The first and essential steps in Wnt secretion are their O-palmitoleation and subsequent loading onto the dedicated transporter Wntless/evenness interrupted (WLS/Evi). We report the 3.2 Å resolution cryogenic electron microscopy (cryo-EM) structure of palmitoleated human WNT8A in complex with WLS. This is accompanied by biochemical experiments to probe the physiological implications of the observed association. The WLS membrane domain has close structural homology to G protein-coupled receptors (GPCRs). A Wnt hairpin inserts into a conserved hydrophobic cavity in the GPCR-like domain, and the palmitoleate protrudes between two helices into the bilayer. A conformational switch of highly conserved residues on a separate Wnt hairpin might contribute to its transfer to receiving cells. This work provides molecular-level insights into a central mechanism in animal body plan development and stem cell biology. PubMed: 33357447DOI: 10.1016/j.cell.2020.11.038 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.19 Å) |
Structure validation
Download full validation report
