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4TNT

Structure of the human mineralocorticoid receptor in complex with DNA

Summary for 4TNT
Entry DOI10.2210/pdb4tnt/pdb
DescriptorMineralocorticoid 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 Keywordsdna binding protein, dna binding protein-dna complex, dna binding protein/dna
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight33247.25
Authors
Hudson, W.H.,Ortlund, E.A. (deposition date: 2014-06-04, release date: 2014-09-17, Last modification date: 2023-12-27)
Primary citationHudson, 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: 25188500
DOI: 10.1371/journal.pone.0107000
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3938 Å)
Structure validation

243911

数据于2025-10-29公开中

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