4TNT
Structure of the human mineralocorticoid receptor in complex with DNA
Summary for 4TNT
| Entry DOI | 10.2210/pdb4tnt/pdb |
| Descriptor | Mineralocorticoid receptor, DNA (5'-D(*CP*AP*GP*AP*AP*CP*AP*CP*TP*CP*TP*GP*TP*TP*CP*TP*G)-3'), DNA (5'-D(*CP*AP*GP*AP*AP*CP*AP*GP*AP*GP*TP*GP*TP*TP*CP*TP*G)-3'), ... (5 entities in total) |
| Functional Keywords | dna binding protein, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 33247.25 |
| Authors | Hudson, W.H.,Ortlund, E.A. (deposition date: 2014-06-04, release date: 2014-09-17, Last modification date: 2023-12-27) |
| Primary citation | Hudson, W.H.,Youn, C.,Ortlund, E.A. Crystal structure of the mineralocorticoid receptor DNA binding domain in complex with DNA. Plos One, 9:e107000-e107000, 2014 Cited by PubMed Abstract: The steroid hormone receptors regulate important physiological functions such as reproduction, metabolism, immunity, and electrolyte balance. Mutations within steroid receptors result in endocrine disorders and can often drive cancer formation and progression. Despite the conserved three-dimensional structure shared among members of the steroid receptor family and their overlapping DNA binding preference, activation of individual steroid receptors drive unique effects on gene expression. Here, we present the first structure of the human mineralocorticoid receptor DNA binding domain, in complex with a canonical DNA response element. The overall structure is similar to the glucocorticoid receptor DNA binding domain, but small changes in the mode of DNA binding and lever arm conformation may begin to explain the differential effects on gene regulation by the mineralocorticoid and glucocorticoid receptors. In addition, we explore the structural effects of mineralocorticoid receptor DNA binding domain mutations found in type I pseudohypoaldosteronism and multiple types of cancer. PubMed: 25188500DOI: 10.1371/journal.pone.0107000 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3938 Å) |
Structure validation
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