par Libert, Frédérick 
;Parmentier, Marc ;Maenhaut, Carine ;Lefort, Anne ;Gérard, Claude ;Perret, Jason ;Van Sande, Jacqueline ;Dumont, Jacques ;Vassart, Gilbert
Référence Molecular and cellular endocrinology, 68, 1, page (R15-R17)
Publication Publié, 1990-01
;Parmentier, Marc ;Maenhaut, Carine ;Lefort, Anne ;Gérard, Claude ;Perret, Jason ;Van Sande, Jacqueline ;Dumont, Jacques ;Vassart, Gilbert Référence Molecular and cellular endocrinology, 68, 1, page (R15-R17)
Publication Publié, 1990-01
Article révisé par les pairs
| Résumé : | A clone coding for a variant form of thyrotropin receptor was isolated from a dog thyroid cDNA library. It was characterized by a 75 bp deletion in the coding region, additionally to minor modifications in the 3' untranslated region. The corresponding 25 amino acids deletion is located in the long NH2 terminal extracellular domain which is characteristic of the glycoprotein hormone receptors. This region of the protein is composed of imperfect repeats and the deletion corresponds exactly to one of the repeat units. This suggests that the repeats correspond to individual exons in the thyrotropin receptor chromosomal gene. It is not known whether the deletion of the repeat and the concomitant suppression of one of the N-glycosylation sites of the molecule do alter the receptor function. |
