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![[Figure 1]](ni5004fig1mag.jpg)
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Figure 1
Schematic overview of the Hedgehog signaling pathway and depiction of key regulatory interfaces. (a) The Hedgehog (Hh) protein N-terminal domain is cleaved by the C-terminal domain, yielding Hh-N products (Shh-N, Dhh-N or Ihh-N signified by the Hh protein), inside Hh-producing cells. Addition of cholesterol to the C-terminus and palmitoylation of the N-terminus produces the active, secreted signaling molecule. Shh-N binding to PTCH1 and the co-receptors CDO and BOC alleviates the inhibition of Smoothened (Smo), allowing the dissociation of Gli proteins from the Kif7 and SuFu proteins. Subsequent activation and transport to the nucleus allows the Gli proteins to carry out activation or repression of transcription, including the upregulation of Hh pathway proteins. (b) Cartoon diagram of the quaternary complex between the FNIII domain of co-receptor CDO, a human homologue of Interference Hedgehog (Ihog), bound to Shh-N (PDB entry 3d1m; McLellan et al., 2008  ). (c) Cartoon diagram of the quaternary complex of the PTCH1 transmembrane receptor bound to Shh-N (PDB entry 6dmy; Gong et al., 2018). (d) Cartoon diagram of the quaternary complex of the HHIP membrane protein bound to Shh-N (PDB entry 2wfx; Bishop et al., 2009). |
![[Figure 1]](ni5004fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
