Progesterone receptor

spinqualitylabelsall models Structure of human progesterone receptor ligand-binding domain complex with RU486 and sulfate (PDB entry 2w8y) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Progesterone receptor (PR) binds to DNA and inhibits transcription. It is nuclear receptor. The inhibition terminates when progesterone binds to PR. The ovarian steroid progesterone which is essential for breast development and reproductive behavior, is mediated by PR. Relevance The response to hormone therapy in breast cancer correlates with PR. PR absence in breast tumor cells predicts resistance to hormone therapy . Structural highlights The structure of the complex of the ligand-binding domain of PR with RU486 - an abortion-inducing drug - shows the ligand bound at a similar location to other agonists or partial agonists with a flexible loop of PR being a possible entry route to the binding site and several PR-RU486 interactions. Water molecules are shown as red spheres.

3D Structures of progesterone receptor

Updated on 25-January-2021

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• Progesterone receptor residues 1-125
  • nuclear receptor – hPR - human
    
• Progesterone receptor residues 72-195
  • 4x8y – hPR
    
• Progesterone receptor DNA-binding domain residues 399-476
  • 2c7a – hPR DBD + DNA
    
• Progesterone receptor ligand-binding domain residues 673-933
  • 3g8o, 3hq5, 3kba, 4a2j, 4apu – hPR LBD + partial agonist
    
  • 1zuc – hPR LBD + agonist
    
  • 1sqn, 3d90 – hPR LBD + contraceptive
    
  • 2w8y – hPR LBD + RU486
    
  • 1a28 – hPR LBD + progesterone
    
  • 1e3k – hPR LBD + metribolone
    
  • 1sr7 – hPR LBD + skin inflammation drug
    
  • 3zr7, 3zra, 3zrb – hPR LBD + modulator
    
  • 2ovh, 2ovm – hPR LBD + modulator + co-repressor peptide
    
  • 4oar – hPR LBD + contraceptive + co-repressor peptide
    

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Michal Harel, Alexander Berchansky