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. Author manuscript; available in PMC: 2019 Apr 1.
Published in final edited form as: Curr Opin Cell Biol. 2017 Dec 18;51:81–88. doi: 10.1016/j.ceb.2017.10.004

Figure 3.

Figure 3

Multi-domain structures of SMO. (a) Close-up of the cholesterol binding site in the SMO CRD. Residues involved in binding are shown as sticks. Dotted black lines indicate potential hydrogen bonds. Two important residues also discussed in the text are labeled (Asp95 and Trp109). (b) Three multi-domain structures of human SMO, each solved with a different ligand (as indicated beneath each structure), are shown in the same orientation (PDB: 5L7D [17••], 5L7I [17••], 5V57 [18••]). The glycan occluding the CRD-site in the vismodegib complex (middle) is shown in yellow stick representation. Domains in (a) and (b) are coloured as in Figure 2. (c) Conformational changes associated with antagonist binding result in collapse of the CRD binding site, thus precluding cholesterol binding. The three multi-domain structures of SMO were aligned by their TMDs. Each structure is coloured separately with helices shown as solid cylinders and loops omitted for clarity. Red arrows indicate domain movements between structures.