Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors.

@article{Guan2010StructuralDU,
  title={Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors.},
  author={Rongbin Guan and Xueqing Wu and Xiuyan Feng and Meilin Zhang and Terence E. H{\'e}bert and Deborah L Segaloff},
  journal={Cellular signalling},
  year={2010},
  volume={22 2},
  pages={247-56}
}
The human follitropin receptor (hFSHR) is a G protein-coupled receptor (GPCR) central to reproductive physiology that is composed of an extracellular domain (ECD) fused to a serpentine region. Using bioluminescence resonance energy transfer (BRET) in living cells, we show that hFSHR dimers form constitutively during their biosynthesis. Mutations in TM1 and TM4 had no effect on hFSHR dimerization, alone or when combined with mutation of Tyr(110) in the ECD, a residue predicted to mediate… CONTINUE READING
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