Supplemental Data

Files in this Data Supplement:

• [Supplemental Table 1] - "Primers used to construct the hFSHR-Ctail Cys mutant cDNAs."
• [Supplemental Figure 1] - "Root mean Square Positional Deviations (RMSD) for the intracellular loops and the Ctail of the Wt hFSHR and Cys mutants (black dashed lines) as a function of the time. RMSD values of the F(X)₆LL motif (red solid lines), are also included. In all cases, the last conformation of the Wt hFSHR was taken as reference structure. Additionally, the starting conformation was employed as a reference structure for the RMSD of the Wt receptor Ctail and intracellular loops (blue line). The lower RMSD of the F(X)₆LL motif for all the trajectories is due to its shorter length when compared to the whole intracellular region of the receptor. Considering the long simulations time scale (~100 ns) and the relatively high temperature (310 K for all mutants except for C627/629/655A that was simulated at 298 K), it is assumed that the probability of finding unrealistic conformations of the simulated residues trapped in local minima of the energy landscape, is reasonably low. The simulation of the C627/629/655A mutant was performed at lower temperature because its structure was particularly unstable. Even under these conditions, no more than ~45 ns could be reached for the trajectory of the triple mutant. The three mutations involving the position 655 (C655A, C655T and C655S) yielded the lowest and most constant RMSD values. Except for the case of the C627A mutant, the RMSD values correlated quite well with data from the plasma membrane expression experiments (see Table 2 and Fig. 5)."
• [Supplemental Movie] - "Movie showing seven ns of the wild-type hFSHR Ctail simulation by using the PS approach described in the text. Chlorine ions (white spheres), water molecules (orange wireframes) and Cys residues at positions 627, 629, and 655 (yellow spheres) are also displayed. The movie is representative of the trajectory after the equilibration time and shows the fluctuations of intracellular loops and the Ctail of the receptor within the partially solvated environment of an average stable structure."