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TitleStructural basis of sterol recognition by human hedgehog receptor PTCH1.
Journal, issue, pagesSci Adv, Vol. 5, Issue 9, Page eaaw6490, Year 2019
Publish dateSep 18, 2019
AuthorsChao Qi / Giulio Di Minin / Irene Vercellino / Anton Wutz / Volodymyr M Korkhov /
PubMed AbstractHedgehog signaling is central in embryonic development and tissue regeneration. Disruption of the pathway is linked to genetic diseases and cancer. Binding of the secreted ligand, Sonic hedgehog ...Hedgehog signaling is central in embryonic development and tissue regeneration. Disruption of the pathway is linked to genetic diseases and cancer. Binding of the secreted ligand, Sonic hedgehog (ShhN) to its receptor Patched (PTCH1) activates the signaling pathway. Here, we describe a 3.4-Å cryo-EM structure of the human PTCH1 bound to ShhN, a modified hedgehog ligand mimicking its palmitoylated form. The membrane-embedded part of PTCH1 is surrounded by 10 sterol molecules at the inner and outer lipid bilayer portion of the protein. The annular sterols interact at multiple sites with both the sterol-sensing domain (SSD) and the SSD-like domain (SSDL), which are located on opposite sides of PTCH1. The structure reveals a possible route for sterol translocation across the lipid bilayer by PTCH1 and homologous transporters.
External linksSci Adv / PubMed:31555730 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.4 Å
Structure data

EMDB-4936, PDB-6rmg:
Structure of PTCH1 bound to a modified Hedgehog ligand ShhN-C24II
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-4939:
Structure of PTCH1 bound to a modified Hedgehog ligand ShhN-C24II: focused refinement of the membrane domain
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-ZN:
Unknown entry

Source
  • eimeria acervulina (eukaryote)
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Patched / PTCH1 / Hedgehog / ShhN

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