6RMG
Structure of PTCH1 bound to a modified Hedgehog ligand ShhN-C24II
Summary for 6RMG
Entry DOI | 10.2210/pdb6rmg/pdb |
EMDB information | 4936 |
Descriptor | Protein 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 Keywords | patched, ptch1, hedgehog, shhn, membrane protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 2 |
Total formula weight | 203194.08 |
Authors | Korkhov, V.M.,Qi, C. (deposition date: 2019-05-06, release date: 2019-10-09, Last modification date: 2024-11-20) |
Primary citation | Qi, 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: 31555730DOI: 10.1126/sciadv.aaw6490 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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