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| [[Image:1a28.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1a28| PDB=1a28 | SCENE= }} | | {{STRUCTURE_1a28| PDB=1a28 | SCENE= }} |
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| '''HORMONE-BOUND HUMAN PROGESTERONE RECEPTOR LIGAND-BINDING DOMAIN'''
| | ===HORMONE-BOUND HUMAN PROGESTERONE RECEPTOR LIGAND-BINDING DOMAIN=== |
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| ==Overview==
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| The physiological effects of progestins are mediated by the progesterone receptor, a member of the steroid/nuclear receptor superfamily. As progesterone is required for maintenance of pregnancy, its receptor has been a target for pharmaceuticals. Here we report the 1.8 A crystal structure of a progesterone-bound ligand-binding domain of the human progesterone receptor. The nature of this structure explains the receptor's selective affinity for progestins and establishes a common mode of recognition of 3-oxy steroids by the cognate receptors. Although the overall fold of the progesterone receptor is similar to that found in related receptors, the progesterone receptor has a quite different mode of dimerization. A hormone-induced stabilization of the carboxy-terminal secondary structure of the ligand-binding domain of the progesterone receptor accounts for the stereochemistry of this distinctive dimer, explains the receptor's characteristic pattern of ligand-dependent protease resistance and its loss of repression, and indicates how the anti-progestin RU486 might work in birth control. The structure also indicates that the analogous 3-keto-steroid receptors may have a similar mechanism of action. | | The line below this paragraph, {{ABSTRACT_PUBMED_9620806}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9620806 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9620806}} |
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| ==Disease== | | ==Disease== |
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| [[Category: Steroid receptor]] | | [[Category: Steroid receptor]] |
| [[Category: Transcription regulation]] | | [[Category: Transcription regulation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:41:59 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:50:25 2008'' |
