Fig. 3: Structural basis for FSHR activation signal transduced from ECD to TMD. | Nature Communications

Fig. 3: Structural basis for FSHR activation signal transduced from ECD to TMD.

From: Mechanism of hormone and allosteric agonist mediated activation of follicle stimulating hormone receptor

Fig. 3

a Structural comparison of FSH-FSHR-Gs complex with CG-LHCGR-Gs and TSH-TSHR- complexes. The similar ECD-TMD configuration in three structures is shown, and the two conserved disulfide bonds in FSHR are shown in sticks. b Structural comparison of the hinge helix in the inactive and active FSHR structures. The angle was measured at the Cα atoms of S273 and R283 from the inactive FSHR and C276 from the active FSHR. c The first conserved interface between hinge helix and ECL1. d Concentration-response curves for WT and S273I mutant receptors. The representative concentration-response curves from three independent experiments were shown. Data were shown as mean ± S.E.M. from three independent experiments. Source data are provided as a Source Data file. e The second conserved interface between P10 and TMD. f Detailed interactions between P10 and FSHR TMD are shown in sticks.

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