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New Naturally Occurring Missense Mutations of the Human Mineralocorticoid Receptor Disclose Important Residues Involved in Dynamic Interactions with Deoxyribonucleic Acid, Intracellular Trafficking, and Ligand Binding
We have investigated the functional consequences of three naturally occurring amino acid substitutions of the human mineralocorticoid receptor (hMR). These mutations are located in the DNAbinding domain and the ligand-binding domain (LBD) and are associated with autosomal dominant or sporadic type I pseudohypoaldosteronism. All mutant receptors bound specifically to glucocorticoid-responsive elements but presented modified transcriptional properties. The DNA-binding domain mutant G633R, whichdoi:10.1210/me.2003-0408 pmid:15192075 fatcat:gkj4o6bgw5a7bgz2zixi7iarse