The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties.
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 the substitution of a valine for a glycine at amino acid position 400 (Gly-400----Val-400). This mutation in the hormone binding domain of the cloned hER destabilizes its structure and decreases its apparent affinity for oestradiol at 25 degrees C, but not at 4 degrees C, when compared with the wild-type hER with a Gly-400.
Tora
L
L
Laboratoire de Génétique Moléculaire des Eucaryotes du CNRS, Faculté de Médecine, Strasbourg, France.
Mullick
A
A
Metzger
D
D
Ponglikitmongkol
M
M
Park
I
I
Chambon
P
P
D001483:Base Sequence; D001943:Breast Neoplasms; D002460:Cell Line; D003001:Cloning, Molecular; D004273:DNA, Neoplasm / Q000235:genetics; D004259:DNA-Directed DNA Polymerase; D005260:Female; D005784:Gene Amplification; D005796:Genes; D005998:Glycine; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D009154:Mutation; D015345:Oligonucleotide Probes; D011960:Receptors, Estrogen / Q000235:genetics* / Q000378:metabolism; D014633:Valine
D004273:DNA, Neoplasm; D015345:Oligonucleotide Probes; D011960:Receptors, Estrogen; D004259:DNA-Directed DNA Polymerase; D014633:Valine; D005998:Glycine