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PMID: 2792078 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The EMBO journal ·Vol. 8 ·No. 7 ·1989-07-00 ·Pages 1981-6

Tora L, Mullick A, Metzger D, Ponglikitmongkol M, Park I, Chambon P

Abstract

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.

MeSH Terms
Base Sequence Breast Neoplasms Cell Line Cloning, Molecular DNA, Neoplasm/genetics DNA-Directed DNA Polymerase Female Gene Amplification Genes Glycine Humans Kinetics Molecular Sequence Data Mutation Oligonucleotide Probes Receptors, Estrogen/genetics,metabolism Valine
Chemicals
DNA, Neoplasm Oligonucleotide Probes Receptors, Estrogen DNA-Directed DNA Polymerase Valine Glycine
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Tora L
Laboratoire de Génétique Moléculaire des Eucaryotes du CNRS, Faculté de Médecine, Strasbourg, France.
Mullick A
Metzger D
Ponglikitmongkol M
Park I
Chambon P
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1989-07-00
Pages
1981-6
Language
English
Region
England
NLM ID
8208664
PMCID
PMC401066
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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