Effects of mutations involving cysteine residues distal to the S281HCC motif at the C-terminus on the functional characteristics of a truncated ectodomain-only thyrotropin receptor anchored on glycosylphosphatidyl-inositol.

@article{Ho2008EffectsOM,
  title={Effects of mutations involving cysteine residues distal to the S281HCC motif at the C-terminus on the functional characteristics of a truncated ectodomain-only thyrotropin receptor anchored on glycosylphosphatidyl-inositol.},
  author={S C Ho and Sui-Sin Goh and Sun M. Li and Daphne Hsu-Chin Khoo and Malcolm C. Paterson},
  journal={Thyroid : official journal of the American Thyroid Association},
  year={2008},
  volume={18 12},
  pages={1313-9}
}
BACKGROUND Cysteine (Cys) residues pair to form disulfide bonds that are important in maintaining structure and function of the thyrotropin receptor (TSHR). There are 11 Cys residues in the ectodomain (ECD). Cys 41 at the N-terminus and Cys 283 at the SHCC motif have been identified as important for ligand binding. The present study evaluated the effects of… CONTINUE READING