The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Determinants for selective RAR and TR recognition of direct repeat HREs.
Open accessAbstract
Recently, we have shown that receptors for vitamin D3 (VDR), thyroid hormone (TR), and retinoic acid (RAR) activate preferentially through direct repeats (DRs) spaced by 3, 4, and 5 nucleotides, respectively. In addition, the RAR can activate weakly through DRs spaced by 2 nucleotides. A common feature of RAR, TR, and VDR is their ability to heterodimerize with the retinoid X receptor (RXR) through their ligand-binding domains (LBDs) to form high-affinity DNA-binding complexes that are specific for appropriately spaced repeats. In this paper we demonstrate that selective binding of RAR-RXR and TR-RXR heterodimers to their cognate DRs is a consequence of a novel cooperative dimer interaction within the DNA-binding domains (DBDs). Accordingly, a region in the first zinc finger of the TR and RAR DBDs interacts with the second zinc finger in the RXR DBD to promote selective DNA-binding to DRs spaced by 4 and 5 nucleotides, respectively. The resulting polarity established by this interaction places RXR in the 5' position of the direct repeats. These data provide a mechanism for selective receptor recognition of a restricted set of target sequences in DR DNA and explains the structural basis for physiological specificity.
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Cites
Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators
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A human retinoic acid receptor which belongs to the family of nuclear receptors
Petkovich, M., Brand, N. J., Krust, A., & Chambon, P. (1987) · Nature · doi:10.1038/330444a0 · Cited by 2,214
Identification of a receptor for the morphogen retinoic acid
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Self-citation9-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
Cited by
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968
Physiological and Molecular Basis of Thyroid Hormone Action
Yen, P. M. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.3.1097 · Cited by 2,011
Endogenous Bile Acids Are Ligands for the Nuclear Receptor FXR/BAR
Wang, H., Chen, J., Hollister, K., Sowers, L. C., & Forman, B. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80348-2 · Cited by 1,636
Nuclear Receptors, RXR, and the Big Bang
Evans, R. M., & Mangelsdorf, D. J. (2014) · Cell · doi:10.1016/j.cell.2014.03.012 · Cited by 1,200
Self-citationLXR, a nuclear receptor that defines a distinct retinoid response pathway.
Willy, P. J., Umesono, K., Ong, E. S., Evans, R. M., Heyman, R. A., & Mangelsdorf, D. J. (1995) · Genes & Development · doi:10.1101/gad.9.9.1033 · Cited by 1,123
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Metadata
- Authors
- Perlmann, T., Rangarajan, P. N., Umesono, K., & Evans, R. M.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1993-07-01
- Volume
- 7
- Issue
- 7b
- Pages
- 1411-1422
- ISSN
- 0890-9369 (ISSN-L)
- OpenAlex
- W1985247182
- Cited by
- 400
- References
- 5
- Type
- posted content
- Language
- en
- Open access
- diamond
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
