Figure 3. Dynamic modeling of hBBSome and Ub‐hBBSome complex.

• A
  Co‐immunoprecipitation assay of BBS1 or BBS1^K143R and BBS3 from lysates of HEK293 transiently expressing the indicated transgenes.
• B
  Cumulative data of the experiments shown in (A). The data are expressed as mean ± SD of three independent experiments. Student's t test, ***P < 0.001.
• C
  Full atomistic description of the homology model of the octameric complex of the BBSome human sequence (hBBSome) in the Arl6^GTP‐bound (open) conformation, with the monoubiquitylation at K143 of hBBS1^4α (Ub‐hBBSome).
• D
  Focus on the full atomistic model of hBBSome core complex components (BBS1, BBS4, BBS8, BBS9, and BBS18).
• E
  Top view of the interaction details between BBS18 α‐helix and the BBS18 U‐bolt domains with the BBS8^TPR and the superhelix of BBS4^TPR, respectively.
• F
  Top view of the interaction details between BBS18 α‐helix with the BBS1^GAE domain and the superhelix of BBS4^TPR.
• G
  Surface representation of the CG‐MD model of the Ub‐hBBSome, representing the starting point of the CG‐MD simulation. Residues involved in the Arl6^GTP‐bound binding mode are highlighted in dark green.
• H, I
  Surface representation of the last CG‐MD frame of the wt‐hBBSome and the Ub‐hBBSome, respectively showing the progressive closure of Arl6‐binding site located between BBS1^βprop and BBS7^βprop. Residues involved in the Arl6^GTP‐bound binding mode are highlighted in red and yellow, respectively.