6TD6
Structure of Drosophila melanogaster Dispatched bound to a modified Hedgehog ligand, HhN-C85II
Summary for 6TD6
Entry DOI | 10.2210/pdb6td6/pdb |
EMDB information | 10452 10464 |
Descriptor | Protein dispatched, Protein hedgehog, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | rnd transporter, dispatched, hedgehog, transmembrane domain, ectodomain, cholesteryl hemisuccinate, detergent micelle, digitonin, monomer, membrane protein |
Biological source | Drosophila melanogaster (Fruit fly) More |
Total number of polymer chains | 2 |
Total formula weight | 192012.61 |
Authors | Korkhov, V.M.,Cannac, F. (deposition date: 2019-11-07, release date: 2020-06-03, Last modification date: 2024-10-23) |
Primary citation | Cannac, F.,Qi, C.,Falschlunger, J.,Hausmann, G.,Basler, K.,Korkhov, V.M. Cryo-EM structure of the Hedgehog release protein Dispatched. Sci Adv, 6:eaay7928-eaay7928, 2020 Cited by PubMed Abstract: The Hedgehog (Hh) signaling pathway controls embryonic development and adult tissue homeostasis in multicellular organisms. In , the pathway is primed by secretion of a dually lipid-modified morphogen, Hh, a process dependent on a membrane-integral protein Dispatched. Although Dispatched is a critical component of the pathway, the structural basis of its activity has, so far, not been described. Here, we describe a cryo-electron microscopy structure of the Dispatched at 3.2-Å resolution. The ectodomains of Dispatched adopt an open conformation suggestive of a receptor-chaperone role. A three-dimensional reconstruction of Dispatched bound to Hh confirms the ability of Dispatched to bind Hh but using a unique mode distinct from those previously observed in structures of Hh complexes. The structure may represent the state of the complex that precedes shedding of Hh from the surface of the morphogen-releasing cell. PubMed: 32494603DOI: 10.1126/sciadv.aay7928 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.76 Å) |
Structure validation
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