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-Structure paper
タイトル | Cryo-EM structure of the Hedgehog release protein Dispatched. |
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ジャーナル・号・ページ | Sci Adv, Vol. 6, Issue 16, Page eaay7928, Year 2020 |
掲載日 | 2020年4月15日 |
![]() | Fabien Cannac / Chao Qi / Julia Falschlunger / George Hausmann / Konrad Basler / Volodymyr M Korkhov / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.16 - 4.76 Å |
構造データ | EMDB-10452, PDB-6tbu: EMDB-10464, PDB-6td6: |
化合物 | ![]() ChemComp-Y01: ![]() ChemComp-NAG: |
由来 |
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![]() | MEMBRANE PROTEIN / RND transporter / transmembrane domain / ectodomain / cholesteryl hemisuccinate / detergent micelle / digitonin / monomer / Dispatched / Hedgehog |