Abstract
Human progesterone receptor (PR) is a member of the nuclear hormone receptor superfamily of transcriptional activators, which share a common modular structure consisting of a C-terminal ligand-binding domain (LBD), a highly conserved and centrally located DNA-binding domain (DBD), and a poorly characterized N-terminal domain that is required for maximal transcriptional activity (1,2) Human PR is expressed as two proteins from a single gene by alternate use of two promoters: PR-A, which is missing the first 164 amino acids in the N-terminus, and full-length PR-B (3).
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Melvin, V.S., Edwards, D.P. (2001). Expression and Purification of Recombinant Human Progesterone Receptor in Baculovirus and Bacterial Systems. In: Lieberman, B.A. (eds) Steroid Receptor Methods. Methods in Molecular Biology™, vol 176. Humana Press. https://doi.org/10.1385/1-59259-115-9:39
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DOI: https://doi.org/10.1385/1-59259-115-9:39
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