Solution structure and characterization of the LGR8 receptor binding surface of insulin-like peptide 3.

@article{Rosengren2006SolutionSA,
  title={Solution structure and characterization of the LGR8 receptor binding surface of insulin-like peptide 3.},
  author={K Johan Rosengren and Suode Zhang and Feng Lin and Norelle L Daly and Daniel J Scott and Richard Anthony Hughes and Ross A D Bathgate and David J. Craik and John D Wade},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 38},
  pages={28287-95}
}
Insulin-like peptide 3 (INSL3), a member of the relaxin peptide family, is produced in testicular Leydig cells and ovarian thecal cells. Gene knock-out experiments have identified a key biological role in initiating testes descent during fetal development. Additionally, INSL3 has an important function in mediating male and female germ cell function. These actions are elicited via its recently identified receptor, LGR8, a member of the leucine-rich repeat-containing G-protein-coupled receptor… CONTINUE READING

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