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TitleTwo Patched molecules engage distinct sites on Hedgehog yielding a signaling-competent complex.
Journal, issue, pagesScience, Vol. 362, Issue 6410, Year 2018
Publish dateOct 5, 2018
AuthorsXiaofeng Qi / Philip Schmiege / Elias Coutavas / Xiaochun Li /
PubMed AbstractAberrant Hedgehog (HH) signaling leads to various types of cancer and birth defects. N-terminally palmitoylated HH initiates signaling by binding its receptor Patched-1 (PTCH1). A recent 1:1 PTCH1-HH ...Aberrant Hedgehog (HH) signaling leads to various types of cancer and birth defects. N-terminally palmitoylated HH initiates signaling by binding its receptor Patched-1 (PTCH1). A recent 1:1 PTCH1-HH complex structure visualized a palmitate-mediated binding site on HH, which was inconsistent with previous studies that implied a distinct, calcium-mediated binding site for PTCH1 and HH co-receptors. Our 3.5-angstrom resolution cryo-electron microscopy structure of native Sonic Hedgehog (SHH-N) in complex with PTCH1 at a physiological calcium concentration reconciles these disparate findings and demonstrates that one SHH-N molecule engages both epitopes to bind two PTCH1 receptors in an asymmetric manner. Functional assays using PTCH1 or SHH-N mutants that disrupt the individual interfaces illustrate that simultaneous engagement of both interfaces is required for efficient signaling in cells.
External linksScience / PubMed:30139912 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

8955

6e1h

EMDB-8955, PDB-6e1h:
Structure of 2:1 human Ptch1-Shh-N complex
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-PLM:
PALMITIC ACID

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / tumor suppressor

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