Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNA

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Abstract

A λgt10 library containing DNAs complementary to messenger RNAs from human breast cancer T47-D cells was constructed and screened with a cDNA probe encoding the rabbit progesterone receptor. Four overlapping clones have been sequenced. The open reading frame corresponds to a protein of 933 amino acids with a molecular weight of 98,868 Da. The cysteine rich basic region supposed to be involved in DNA binding is completely homologous in the human and rabbit receptors, whereas the C-terminal end, where hormone binding is thought to take place, differs by a single amino acid change. The human progesterone receptor is characterized, as is the rabbit receptor, by the very high proline content of its N-terminal region. When mRNAs from either human breast cancer cell lines T47-D and MCF-7 or from normal human uterus tissue were blotted and probed with the cloned cDNA, four main bands were observed (5100, 4300, 3700, and 2900 nucleotides). © 1987.

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Misrahi, M., Atger, M., d’Auriol, L., Loosfelt, H., Meriel, C., Fridlansky, F., … Milgrom, E. (1987). Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNA. Biochemical and Biophysical Research Communications, 143(2), 740–748. https://doi.org/10.1016/0006-291X(87)91416-1

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