Nuclear receptors: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
Line 21: | Line 21: | ||
===[[Liver X receptor]]=== | ===[[Liver X receptor]]=== | ||
===[[Bile acid receptor]] (Farnesoid X receptor)=== | ===[[Bile acid receptor]] (Farnesoid X receptor)=== | ||
==Vitamin D receptor-like== | ==Vitamin D receptor-like== | ||
===[[Vitamin D receptor]]=== | ===[[Vitamin D receptor]]=== | ||
Line 43: | Line 44: | ||
===[[Progesterone receptor]]=== | ===[[Progesterone receptor]]=== | ||
===[[Androgen receptor]]=== | ===[[Androgen receptor]]=== | ||
=[[Liver receptor homolog-1]]?= | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 15:34, 24 February 2021
Under development!!! Nuclear receptor structure is composed of 5 domains - A/B: N-terminal regulatory domain contains activation function 1 (residues 101-370), activation function 5 (residues 360-485) and dimerization surface (residues 1-36 and 370-494). Family members (~ according to [1]): Thyroid Hormone Receptor-likeThyroid hormone receptorRetinoic acid receptorRA Mediated T-reg Differentiation; Retinoic acid acts as the ligand for the Retinoic Acid Receptor-α (RARα) / Retinoid X Receptor-α (RXRα) heterodimerPeroxisome Proliferator-Activated ReceptorsPPARγ
Liver X receptor-likeLiver X receptorBile acid receptor (Farnesoid X receptor)Vitamin D receptor-likeVitamin D receptorPregnane X receptor
Retinoid X Receptor-likeRetinoid X receptorRA Mediated T-reg Differentiation; Retinoic acid acts as the ligand for the Retinoic Acid Receptor-α (RARα) / Retinoid X Receptor-α (RXRα) heterodimerEstrogen Receptor-likeEstrogen receptorEstrogen receptor alpha
Estrogen receptor beta3-Ketosteroid receptorsGlucocorticoid receptorMineralocorticoid receptorProgesterone receptorAndrogen receptorLiver receptor homolog-1? |
|
ReferencesReferences
- ↑ Bohl CE, Wu Z, Chen J, Mohler ML, Yang J, Hwang DJ, Mustafa S, Miller DD, Bell CE, Dalton JT. Effect of B-ring substitution pattern on binding mode of propionamide selective androgen receptor modulators. Bioorg Med Chem Lett. 2008 Oct 15;18(20):5567-70. Epub 2008 Sep 5. PMID:18805694 doi:10.1016/j.bmcl.2008.09.002
- ↑ Li MJ, Greenblatt HM, Dym O, Albeck S, Pais A, Gunanathan C, Milstein D, Degani H, Sussman JL. Structure of estradiol metal chelate and estrogen receptor complex: The basis for designing a new class of selective estrogen receptor modulators. J Med Chem. 2011 Apr 7. PMID:21473635 doi:10.1021/jm200192y