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• W2034607609 endingPage "1121" @default.
• W2034607609 startingPage "1117" @default.
• W2034607609 abstract "The three-dimensional solution structure of the DNA binding domain (DBD) of the retinoid X receptor alpha (RXR alpha) was determined by nuclear magnetic resonance spectroscopy. The two zinc fingers of the RXR DBD fold to form a single structural domain that consists of two perpendicularly oriented helices and that resembles the corresponding regions of the glucocorticoid and estrogen receptors (GR and ER, respectively). However, in contrast to the DBDs of the GR and ER, the RXR DBD contains an additional helix immediately after the second zinc finger. This third helix mediates both protein-protein and protein-DNA interactions required for cooperative, dimeric binding of the RXR DBD to DNA. Identification of the third helix in the RXR DBD thus defines a structural feature required for selective dimerization of the RXR on hormone response elements composed of half-sites (5'-AGGTCA-3') arranged as tandem repeats." @default.
• W2034607609 created "2016-06-24" @default.
• W2034607609 creator A5023246864 @default.
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• W2034607609 date "1993-05-21" @default.
• W2034607609 modified "2023-10-16" @default.
• W2034607609 title "Structure of the Retinoid X Receptor α DNA Binding Domain: a Helix Required for Homodimeric DNA Binding" @default.
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• W2034607609 doi "https://doi.org/10.1126/science.8388124" @default.
• W2034607609 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8388124" @default.
• W2034607609 hasPublicationYear "1993" @default.
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