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6TD6

Structure of Drosophila melanogaster Dispatched bound to a modified Hedgehog ligand, HhN-C85II

Summary for 6TD6
Entry DOI10.2210/pdb6td6/pdb
EMDB information10452 10464
DescriptorProtein dispatched, Protein hedgehog, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsrnd transporter, dispatched, hedgehog, transmembrane domain, ectodomain, cholesteryl hemisuccinate, detergent micelle, digitonin, monomer, membrane protein
Biological sourceDrosophila melanogaster (Fruit fly)
More
Total number of polymer chains2
Total formula weight192012.61
Authors
Korkhov, V.M.,Cannac, F. (deposition date: 2019-11-07, release date: 2020-06-03, Last modification date: 2024-10-23)
Primary citationCannac, 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: 32494603
DOI: 10.1126/sciadv.aay7928
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.76 Å)
Structure validation

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