The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties.

摘要: We demonstrate here that the human oestrogen receptor (hER) cDNA clone pOR8 obtained from MCF-7 cells contains an artefactual point mutation which results in substitution of a valine for glycine at amino acid position 400 (Gly-400----Val-400). This hormone binding domain cloned hER destabilizes its structure and decreases apparent affinity oestradiol 25 degrees C, but not 4 when compared with wild-type Gly-400.