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Progesterone receptor
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Progesterone receptor
The progesterone receptor (PR), also known as NR3C3 or nuclear receptor subfamily 3, group C, member 3, is a protein found inside cells. It is activated by the steroid hormone progesterone.
In humans, PR is encoded by a single PGR gene residing on chromosome 11q22, it has three isoforms: PR-A, PR-B, and PR-C. Though PR-A and PR-B are much more well studied compared to PR-C. The PR-B is the positive regulator of the effects of progesterone, while PR-A serve to antagonize the effects of PR-B.
Progesterone is necessary to induce activation of the progesterone receptors. When no binding hormone is present the carboxyl terminal inhibits transcription. Binding to a hormone induces a structural change that removes the inhibitory action. Progesterone antagonists prevent the structural reconfiguration.
After progesterone binds to the receptor, restructuring with dimerization follows and the complex enters the nucleus and binds to DNA. There transcription takes place, resulting in formation of messenger RNA that is translated by ribosomes to produce specific proteins.
In common with other steroid receptors, the progesterone receptor has a N-terminal regulatory domain, a DNA binding domain, a hinge section, and a C-terminal ligand binding domain. A special transcription activation function (TAF), called TAF3, is present in the progesterone receptor-B, in a B-upstream segment (BUS) at the amino acid terminal. This segment is not present in the receptor-A.
The single-copy human (hPR) gene uses separate promoters and translational start sites to produce three isoforms, PR-A, -B, and -C. PR-A and -B are identical except for an additional 165 amino acids present only in the N terminus of PR-B. PR-C is even smaller, starting at the 595th amino acid of PR-B. Although the three isoforms share many important structural domains, they are functionally distinct.
PR-A and PR-B are disticnt transcription factors, which mediate their own response genes and physiological effects with little overlap.
PR-C being the smallest, does not have the important AF1, AF3, or DNA-binding domains. Thus, PR-C is not a transcription factor. However, PR-C can dimerize, participate in nuclear translocation, and modulate the actions of PR-A and PR-B.
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Progesterone receptor
The progesterone receptor (PR), also known as NR3C3 or nuclear receptor subfamily 3, group C, member 3, is a protein found inside cells. It is activated by the steroid hormone progesterone.
In humans, PR is encoded by a single PGR gene residing on chromosome 11q22, it has three isoforms: PR-A, PR-B, and PR-C. Though PR-A and PR-B are much more well studied compared to PR-C. The PR-B is the positive regulator of the effects of progesterone, while PR-A serve to antagonize the effects of PR-B.
Progesterone is necessary to induce activation of the progesterone receptors. When no binding hormone is present the carboxyl terminal inhibits transcription. Binding to a hormone induces a structural change that removes the inhibitory action. Progesterone antagonists prevent the structural reconfiguration.
After progesterone binds to the receptor, restructuring with dimerization follows and the complex enters the nucleus and binds to DNA. There transcription takes place, resulting in formation of messenger RNA that is translated by ribosomes to produce specific proteins.
In common with other steroid receptors, the progesterone receptor has a N-terminal regulatory domain, a DNA binding domain, a hinge section, and a C-terminal ligand binding domain. A special transcription activation function (TAF), called TAF3, is present in the progesterone receptor-B, in a B-upstream segment (BUS) at the amino acid terminal. This segment is not present in the receptor-A.
The single-copy human (hPR) gene uses separate promoters and translational start sites to produce three isoforms, PR-A, -B, and -C. PR-A and -B are identical except for an additional 165 amino acids present only in the N terminus of PR-B. PR-C is even smaller, starting at the 595th amino acid of PR-B. Although the three isoforms share many important structural domains, they are functionally distinct.
PR-A and PR-B are disticnt transcription factors, which mediate their own response genes and physiological effects with little overlap.
PR-C being the smallest, does not have the important AF1, AF3, or DNA-binding domains. Thus, PR-C is not a transcription factor. However, PR-C can dimerize, participate in nuclear translocation, and modulate the actions of PR-A and PR-B.
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