1a28
From Proteopedia
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'''HORMONE-BOUND HUMAN PROGESTERONE RECEPTOR LIGAND-BINDING DOMAIN''' | '''HORMONE-BOUND HUMAN PROGESTERONE RECEPTOR LIGAND-BINDING DOMAIN''' | ||
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[[Category: Sigler, P B.]] | [[Category: Sigler, P B.]] | ||
[[Category: Williams, S P.]] | [[Category: Williams, S P.]] | ||
| - | [[Category: | + | [[Category: Nuclear receptor]] |
| - | [[Category: | + | [[Category: Progesterone receptor]] |
| - | [[Category: | + | [[Category: Steroid receptor]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 06:41, 2 May 2008
HORMONE-BOUND HUMAN PROGESTERONE RECEPTOR LIGAND-BINDING DOMAIN
Contents |
Overview
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.
Disease
Known disease associated with this structure: Progesterone resistance, 264080 (2) OMIM:[607311]
About this Structure
1A28 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Atomic structure of progesterone complexed with its receptor., Williams SP, Sigler PB, Nature. 1998 May 28;393(6683):392-6. PMID:9620806 Page seeded by OCA on Fri May 2 09:41:59 2008
