Crystal structure of a mutant mineralocorticoid receptor responsible for hypertension

Jérôme Fagart; Jessica Huyet; Grégory M. Pinon; Marina Rochel; Claudine Mayer; Marie Edith Rafestin-Oblin

doi:10.1038/nsmb939

Crystal structure of a mutant mineralocorticoid receptor responsible for hypertension

Jérôme Fagart
, Jessica Huyet
, Grégory M. Pinon
, Marina Rochel
, Claudine Mayer
, Marie Edith Rafestin-Oblin

INSERM U869
AP-HP

Résultats de recherche: Contribution à un journal › Article › Revue par des pairs

Résumé

The S810L mutation within the human mineralocorticoid receptor (MR S810L) induces severe hypertension and switches progesterone from antagonist to agonist. Here we report the crystal structures of the ligand-binding domain of MR S810L in complex with progesterone and deoxycorticosterone, an agonist of both wild-type and mutant MRs. These structures, the first for MR, identify the specific contacts created by Leu810 and clarify the mechanism of activation of MR S810L.

langue originale	Anglais
Pages (de - à)	554-555
Nombre de pages	2
journal	Nature Structural and Molecular Biology
Volume	12
Numéro de publication	6
Les DOIs	https://doi.org/10.1038/nsmb939
état	Publié - 1 janv. 2005
Modification externe	Oui

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10.1038/nsmb939

Contient cette citation

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abstract = "The S810L mutation within the human mineralocorticoid receptor (MR S810L) induces severe hypertension and switches progesterone from antagonist to agonist. Here we report the crystal structures of the ligand-binding domain of MR S810L in complex with progesterone and deoxycorticosterone, an agonist of both wild-type and mutant MRs. These structures, the first for MR, identify the specific contacts created by Leu810 and clarify the mechanism of activation of MR S810L.",

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AU - Fagart, Jérôme

AU - Huyet, Jessica

AU - Pinon, Grégory M.

AU - Rochel, Marina

AU - Mayer, Claudine

AU - Rafestin-Oblin, Marie Edith

PY - 2005/1/1

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N2 - The S810L mutation within the human mineralocorticoid receptor (MR S810L) induces severe hypertension and switches progesterone from antagonist to agonist. Here we report the crystal structures of the ligand-binding domain of MR S810L in complex with progesterone and deoxycorticosterone, an agonist of both wild-type and mutant MRs. These structures, the first for MR, identify the specific contacts created by Leu810 and clarify the mechanism of activation of MR S810L.

AB - The S810L mutation within the human mineralocorticoid receptor (MR S810L) induces severe hypertension and switches progesterone from antagonist to agonist. Here we report the crystal structures of the ligand-binding domain of MR S810L in complex with progesterone and deoxycorticosterone, an agonist of both wild-type and mutant MRs. These structures, the first for MR, identify the specific contacts created by Leu810 and clarify the mechanism of activation of MR S810L.

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DO - 10.1038/nsmb939

M3 - Article

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SP - 554

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Crystal structure of a mutant mineralocorticoid receptor responsible for hypertension

Résumé

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