30 YEARS OF THE MINERALOCORTICOID RECEPTOR: Mineralocorticoid receptor mutations
- 1INSERM, Paris Cardiovascular Research Center, Paris, France
- 2Université Paris Descartes, Sorbonne Paris Cité, Paris, France
- 3Assistance Publique-Hôpitaux de Paris, Hôpital Européen Georges Pompidou, Service de Génétique, Paris, France
- Correspondence should be addressed to M-C Zennaro; Email: maria-christina.zennaro{at}inserm.fr
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Figure 1
Three-dimensional homology model of the MR LBD. (A) Overall structure of the MR LBD, α-helices are drawn as ribbons and β-strands as arrows. Aldosterone is inserted into the ligand-binding pocket (carbon atoms are in white and oxygen atoms in red). (B) Linear scheme indicating amino acids of the MR LBD-contacting aldosterone. Hydrogen bonds are depicted as arrows, van der Waals contacts as dashed lines. W, water molecule. Reprinted from Molecular and Cellular Endocrinology, Volume 350, Huyet J, Pinon GM, Fay MR, Rafestin-Oblin ME & Fagart J, Structural determinants of ligand binding to the mineralocorticoid receptor, pages 187–195. Copyright 2012, with permission from Elsevier.
- © 2017 Society for Endocrinology
