Premium
The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties.
Author(s) -
Tora L.,
Mullick A.,
Metzger D.,
Ponglikitmongkol M.,
Park I.,
Chambon P.
Publication year - 1989
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1989.tb03604.x
Subject(s) - biology , point mutation , mutation , complementary dna , amino acid , valine , microbiology and biotechnology , receptor , glycine , peptide sequence , binding site , biochemistry , gene
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.