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TitleStructure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis.
Journal, issue, pagesLife Sci Alliance, Vol. 3, Issue 8, Year 2020
Publish dateJul 9, 2020
AuthorsHongwen Chen / Yang Liu / Xiaochun Li /
PubMed AbstractHedgehog (HH) signaling is essential for metazoan development. The HH ligand is secreted into the extracellular space by a cell surface protein named Dispatched-1 (DISP1). Here, we report the cryo-EM ...Hedgehog (HH) signaling is essential for metazoan development. The HH ligand is secreted into the extracellular space by a cell surface protein named Dispatched-1 (DISP1). Here, we report the cryo-EM structure of human DISP1 protein. DISP1 contains 12 transmembrane helices (TMs) and two extracellular domains (ECDs). Its ECDs reveal an open state, in contrast to its structural homologues PTCH1 and NPC1, whose extracellular/luminal domains adopt a closed state. The low-resolution structure of the DISP1 complex with dual lipid-modified HH ligand reveals how the ECDs of DISP1 engage with HH ligand. Moreover, several cholesterol-like molecules are found in the TMs, implying a transport-like function of DISP1.
External linksLife Sci Alliance / PubMed:32646883 / PubMed Central
MethodsEM (single particle)
Resolution4.53 Å
Structure data

22144

6xe6

EMDB-22144, PDB-6xe6:
Structure of Human Dispatched-1 (DISP1)
Method: EM (single particle) / Resolution: 4.53 Å

Chemicals

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / hedgehog / secretion / sterol binding / Sterol-sensing domain

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