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Progesterone receptor

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== Structural highlights ==
== Structural highlights ==
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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 <scene name='78/780972/Cv/4'>binding site and several PR-RU486 interactions</scene><ref>PMID:19372222</ref>. Water molecules are shown as red spheres.
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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 <scene name='78/780972/Cv/4'>binding site and several PR-RU486 interactions</scene><ref>PMID:19372222</ref>. Water molecules are shown as red spheres. <scene name='89/895670/Cv/8'>Human progesterone receptor ligand-binding domain bound with progesterone</scene> ([[1a28]]).
</StructureSection>
</StructureSection>
== 3D Structures of progesterone receptor ==
== 3D Structures of progesterone receptor ==

Revision as of 13:55, 14 November 2021

Structure of human progesterone receptor ligand-binding domain complex with RU486 and sulfate (PDB entry 2w8y)

Drag the structure with the mouse to rotate

3D Structures of progesterone receptor

Updated on 14-November-2021

References

  1. ↑ Lange CA, Yee D. Progesterone and breast cancer. Womens Health (Lond). 2008 Mar;4(2):151-62. doi: 10.2217/17455057.4.2.151. PMID:19072517 doi:http://dx.doi.org/10.2217/17455057.4.2.151
  2. ↑ Cui X, Schiff R, Arpino G, Osborne CK, Lee AV. Biology of progesterone receptor loss in breast cancer and its implications for endocrine therapy. J Clin Oncol. 2005 Oct 20;23(30):7721-35. doi: 10.1200/JCO.2005.09.004. PMID:16234531 doi:http://dx.doi.org/10.1200/JCO.2005.09.004
  3. ↑ Raaijmakers HC, Versteegh JE, Uitdehaag JC. The X-ray structure of RU486 bound to the progesterone receptor in a destabilized agonistic conformation. J Biol Chem. 2009 Jul 17;284(29):19572-9. Epub 2009 Apr 16. PMID:19372222 doi:http://dx.doi.org/10.1074/jbc.M109.007872

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Michal Harel, Alexander Berchansky

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