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6RMG

Structure of PTCH1 bound to a modified Hedgehog ligand ShhN-C24II

Summary for 6RMG
Entry DOI10.2210/pdb6rmg/pdb
EMDB information4936
DescriptorProtein patched homolog 1,GFP-like fluorescent chromoprotein FP506, related, Sonic hedgehog protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordspatched, ptch1, hedgehog, shhn, membrane protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight203194.08
Authors
Korkhov, V.M.,Qi, C. (deposition date: 2019-05-06, release date: 2019-10-09, Last modification date: 2024-11-20)
Primary citationQi, C.,Di Minin, G.,Vercellino, I.,Wutz, A.,Korkhov, V.M.
Structural basis of sterol recognition by human hedgehog receptor PTCH1.
Sci Adv, 5:eaaw6490-eaaw6490, 2019
Cited by
PubMed Abstract: 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.
PubMed: 31555730
DOI: 10.1126/sciadv.aaw6490
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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