6XTZ
Structure of Dally-like protein in complex with O-palmitoleoyl serine
Summary for 6XTZ
| Entry DOI | 10.2210/pdb6xtz/pdb |
| Descriptor | Dally-like, isoform A, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total) |
| Functional Keywords | glypicans, gpi-anchored, wnt, palmitoleate, signaling protein |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 63795.39 |
| Authors | Vecchia, L.,Jones, E.Y. (deposition date: 2020-01-16, release date: 2020-07-29, Last modification date: 2024-10-16) |
| Primary citation | McGough, I.J.,Vecchia, L.,Bishop, B.,Malinauskas, T.,Beckett, K.,Joshi, D.,O'Reilly, N.,Siebold, C.,Jones, E.Y.,Vincent, J.P. Glypicans shield the Wnt lipid moiety to enable signalling at a distance. Nature, 585:85-90, 2020 Cited by PubMed Abstract: A relatively small number of proteins have been suggested to act as morphogens-signalling molecules that spread within tissues to organize tissue repair and the specification of cell fate during development. Among them are Wnt proteins, which carry a palmitoleate moiety that is essential for signalling activity. How a hydrophobic lipoprotein can spread in the aqueous extracellular space is unknown. Several mechanisms, such as those involving lipoprotein particles, exosomes or a specific chaperone, have been proposed to overcome this so-called Wnt solubility problem. Here we provide evidence against these models and show that the Wnt lipid is shielded by the core domain of a subclass of glypicans defined by the Dally-like protein (Dlp). Structural analysis shows that, in the presence of palmitoleoylated peptides, these glypicans change conformation to create a hydrophobic space. Thus, glypicans of the Dlp family protect the lipid of Wnt proteins from the aqueous environment and serve as a reservoir from which Wnt proteins can be handed over to signalling receptors. PubMed: 32699409DOI: 10.1038/s41586-020-2498-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.21 Å) |
Structure validation
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