@article{a591e3e054ad11dd8d9f000ea68e967b,
title = "Characterization of the hormone-binding domain of the chicken c-erbA/thyroid hormone receptor protein.",
abstract = "To identify and characterize the hormone-binding domain of the thyroid hormone receptor, we analyzed the ligand-binding capacities of proteins representing chimeras between the normal receptor and P75gag-v-erbA, the retrovirus-encoded form deficient in binding ligand. Our results show that several mutations present in the carboxy-terminal half of P75gag-v-erbA co-operate in abolishing hormone binding, and that the ligand-binding domain resides in a position analogous to that of steroid receptors. Furthermore, a point mutation that is located between the putative DNA and ligand-binding domains of P75gag-v-erbA and that renders it biologically inactive fails to affect hormone binding by the c-erbA protein. These results suggest that the mutation changed the ability of P75gag-v-erbA to affect transcription since it also had no effect on DNA binding. Our data also suggest that hormone-independent activity of P75gag-v-erbA provided a selective advantage to the avian erythroblastosis virus during the original selection for a highly oncogenic strain of the virus.",
author = "A Mu{\~n}oz and M Zenke and U Gehring and J Sap and H Beug and B Vennstr{\"o}m",
note = "Keywords: Animals; Chickens; Chimera; Cloning, Molecular; Genes; Kinetics; Mutation; Plasmids; Protein Biosynthesis; Proto-Oncogenes; Receptors, Thyroid Hormone; Recombinant Proteins; Thyroid Hormones; Transcription, Genetic",
year = "1988",
language = "English",
volume = "7",
pages = "155--9",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "1",
}