The first cysteine-rich domain of the receptor GFRalpha1 stabilizes the binding of GDNF.

@article{Virtanen2005TheFC,
  title={The first cysteine-rich domain of the receptor GFRalpha1 stabilizes the binding of GDNF.},
  author={Heidi Virtanen and Jianmin Yang and Maxim M. Bespalov and Jukka O Hiltunen and Veli-Matti Lepp{\"a}nen and Nisse Erkki Juhani Kalkkinen and Adrian Goldman and Mart Saarma and Pia Runeberg-Roos},
  journal={The Biochemical journal},
  year={2005},
  volume={387 Pt 3},
  pages={
          817-24
        }
}
The GDNF (glial cell line-derived neurotrophic factor)-binding receptor GFRalpha1 (GDNF family receptor alpha1) is attached to the membrane by a GPI (glycosylphosphatidylinositol) anchor and consists of three cysteine-rich domains. The region corresponding to the second and third domains has been shown previously to participate in ligand binding, and to interact with the transmembrane tyrosine kinase receptor RET. No function has so far been found for the N-terminal, first domain (D1). Here we… CONTINUE READING

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