COMPLETE AMINO-ACID-SEQUENCE OF THE HUMAN PROGESTERONE-RECEPTOR DEDUCED FROM CLONED CDNA
COMPLETE AMINO-ACID-SEQUENCE OF THE HUMAN PROGESTERONE-RECEPTOR DEDUCED FROM CLONED CDNA
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DOI:
10.1016/0006-291x(87)91416-1
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发表时间:
1987-03-13
影响因子:
3.1
通讯作者:
MILGROM, E
中科院分区:
文献类型:
--
作者:
MISRAHI, M;ATGER, M;MILGROM, E
A .lambda.gt10 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).