The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Structure of the Retinoid X Receptor α DNA Binding Domain: a Helix Required for Homodimeric DNA Binding
Abstract
The three-dimensional solution structure of the DNA binding domain (DBD) of the retinoid X receptor α (RXRα) 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.
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Cites
9-cis retinoic acid is a high affinity ligand for the retinoid X receptor
Heyman, R. A., Mangelsdorf, D. J., Dyck, J. A., Stein, R. B., Eichele, G., Evans, R. M., & Thaller, C. (1992) · Cell · doi:10.1016/0092-8674(92)90479-v · Cited by 1,780
Self-citationCrystallographic analysis of the interaction of the glucocorticoid receptor with DNA
Luisi, B. F., Xu, W. X., Otwinowski, Z., Freedman, L. P., Yamamoto, K. R., & Sigler, P. B. (1991) · Nature · doi:10.1038/352497a0 · Cited by 1,503
Oro, A. E., McKeown, M., & Evans, R. M. (1990) · Nature · doi:10.1038/347298a0 · Cited by 406
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Cited by
Nuclear retinoid receptors and the transcription of retinoid-target genes
Bastien, J., & Rochette-Egly, C. (2004) · Gene · doi:10.1016/j.gene.2003.12.005 · Cited by 773
Schwabe, J. W. R., Chapman, L., Finch, J. T., & Rhodes, D. (1993) · Cell · doi:10.1016/0092-8674(93)90390-c · Cited by 750
Ecdysone receptors and their biological actions
Riddiford, L. M., Cherbas, P., & Truman, J. W. (2000) · Vitamins & Hormones · doi:10.1016/s0083-6729(00)60016-x · Cited by 605
Laudet, V (1997) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0190207 · Cited by 557
Peroxisome proliferator-activated receptors: insight into multiple cellular functions
Escher, P., & Wahli, W. (2000) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/s0027-5107(99)00231-6 · Cited by 491
Metadata
- Authors
- Lee, M. S., Kliewer, S. A., Provencal, J., Wright, P. E., & Evans, R. M.
- Venue
- Science
- Published
- 1993-05-21
- Volume
- 260
- Issue
- 5111
- Pages
- 1117-1121
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2034607609
- Cited by
- 292
- References
- 3
- FWCI
- 12.12
- Type
- journal article
- Language
- en
- Open access
- closed
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- Lee, M. S., Kliewer, S. A., Provencal, J., Wright, P. E., & Evans, R. M. (1993). Structure of the Retinoid X Receptor α DNA Binding Domain: a Helix Required for Homodimeric DNA Binding. Science. https://doi.org/10.1126/science.8388124
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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