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

Authors :
Daniel Metzger
Mathurose Ponglikitmongkol
Laszlo Tora
I. Park
A. Mullick
Pierre Chambon
Laboratoire de Génetique Moléculaire des Eucaryotes (LGME)
Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)
Source :
Europe PubMed Central, Scopus-Elsevier, EMBO Journal, EMBO Journal, EMBO Press, 1989, 8 (7), pp.1981-6

Abstract

International audience; 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.

Details

ISSN :
02614189 and 14602075
Database :
OpenAIRE
Journal :
Europe PubMed Central, Scopus-Elsevier, EMBO Journal, EMBO Journal, EMBO Press, 1989, 8 (7), pp.1981-6
Accession number :
edsair.doi.dedup.....89bb99e4ba6c36b91e33b19b6c078631