The six N-linked carbohydrates of the lutropin/choriogonadotropin receptor are not absolutely required for correct folding, cell surface expression, hormone binding, or signal transduction.

@article{Davis1997TheSN,
  title={The six N-linked carbohydrates of the lutropin/choriogonadotropin receptor are not absolutely required for correct folding, cell surface expression, hormone binding, or signal transduction.},
  author={David P. Davis and T G Rozell and Xiaowen Liu and Deborah L Segaloff},
  journal={Molecular endocrinology},
  year={1997},
  volume={11 5},
  pages={550-62}
}
Using two separate methods, we have determined that all six potential sites for N-linked glycosylation on the rat lutropin/choriogonadotropin receptor (rLHR) contain carbohydrates. The functional roles of the carbohydrates were analyzed initially through the use of two nonglycosylated receptor mutants rLHR(N(77,152,173,269,277,291)Q) and rLHR(N(77,152,269,277,291)Q;T(175)A). Although Western blot analyses demonstrated both mutant receptors to be stably expressed, little or no hCG binding… CONTINUE READING

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