Mineralocorticoid receptor: Difference between revisions

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<StructureSection load='2aa2' size='400' side='right' caption='Glycosylated human mineralocorticoid receptor ligand-binding domain complex with aldosterone, glycerol and sulfate (PDB entry [[2aa2]])' scene='78/781019/Cv/1'>
<StructureSection load='' size='350' side='right' caption='Glycosylated human mineralocorticoid receptor ligand-binding domain complex with aldosterone, glycerol and sulfate (PDB entry [[2aa2]])' scene='78/781019/Cv/1'>




== Function ==
== Function ==


'''Mineralocorticoid receptor''' (MR) in epithelial cells is activated by the mineralocorticoid hormone aldosterone promoting renal sodium retention and potassium excretion. In non epithelial cells MR is activated by cortisol<ref>PMID:15199296</ref>.  MR is exposed to many steroids including cortisol, cortisone and progesterone, however, aldosterone and deoxycorticosterone are its physiological ligands.
'''Mineralocorticoid receptor''' (MR) in epithelial cells is activated by the mineralocorticoid hormone aldosterone promoting renal sodium retention and potassium excretion. It is [[Nuclear receptors|nuclear receptor]]. In non epithelial cells MR is activated by cortisol<ref>PMID:15199296</ref>.  MR is exposed to many steroids including cortisol, cortisone and progesterone, however, aldosterone and deoxycorticosterone are its physiological ligands.
 
See also [[Mineralocorticoids]]; [[Steroid Hormones and their receptors]] and [[Intracellular receptors]]


== Disease ==
== Disease ==
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== Structural highlights ==
== Structural highlights ==


The MR ligand aldosterone binds in a fully enclosed pocket, contacting residues with six α-helices and a β-turn.  It forms hydrogen bonds with 4 MR residues<ref>PMID:15967794</ref>.
The MR ligand aldosterone binds in a <scene name='78/781019/Cv/6'>fully enclosed pocket, contacting residues with six α-helices and a β-turn</scene> ({{Template:ColorKey_Helix}}, {{Template:ColorKey_Strand}}, {{Template:ColorKey_Loop}},
{{Template:ColorKey_Turn}})<scene name='78/781019/Cv/7'>It forms hydrogen bonds with 4 MR residues</scene><ref>PMID:15967794</ref>. <scene name='78/781019/Cv/8'>Whole binding site</scene>. Water molecules are shown as red spheres.


</StructureSection>
</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|


*Mineralocorticoid receptor DNA-binding site residues 593-
*Mineralocorticoid receptor DNA-binding site residues 593-671
671


**[[4tnt]] – hMR DBD + DNA - human<br />
**[[4tnt]] – hMR DBD + DNA - human<br />
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**[[2ab2]], [[3vhu]], [[2oax]] – hMR LBD (mutant) + spironolactone <br />
**[[2ab2]], [[3vhu]], [[2oax]] – hMR LBD (mutant) + spironolactone <br />
**[[3wff]], [[3wfg]], [[4pf3]], [[3vhv]], [[5hcv]] – hMR LBD (mutant) + antagonist <br />
**[[3wff]], [[3wfg]], [[4pf3]], [[3vhv]], [[5hcv]] – hMR LBD (mutant) + antagonist <br />
**[[2a3i]] – hMR LBD (mutant) + NCOA1 peptide <br />
**[[6l88]] – hMR LBD (mutant) + esaxerenone<br />
**[[5l7e]], [[5l7g]], [[5l7h]], [[4uda]], [[4udb]] – hMR LBD + NCOA1 peptide + antagonist<br />
**[[5mwy]], [[6gev]] – hMR LBD + NCOA1 peptide <br />
**[[2a3i]], [[5mwp]] – hMR LBD (mutant) + NCOA1 peptide <br />
**[[5l7e]], [[5l7g]], [[5l7h]], [[4uda]], [[4udb]], [[6gg8]], [[6ggg]] – hMR LBD + NCOA1 peptide + antagonist<br />
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman