Article
Cysteine 390 mutation of the TSH receptor modulates its ectodomain as an inverse agonist on the serpentine domain with decrease in basal constitutive activity.
Molecular and cellular endocrinology - 21 Dec 2005
Ho Su-Chin, Goh Sui-Sin, Su Qing, Khoo Daphne Hsu-Chin
Abstract excerpt
Mutations of individual cysteine residues at codon 301, 390, 398 and 408 of the thyrotropin receptor (TSHr) to serine resulted in cell surface expression of only C301S and C390S mutants. C390S mutation was a silencing mutation with decreased basal constitutive activity. Although the C301S and C390S mutants did not show any significant TSH binding, they generated cyclic AMP upon TSH stimulation. These mutants were...
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