ArticleProceedings of the National Academy of Sciences of the United States of America1995
The N-terminal portion of domain E of retinoic acid receptors alpha and beta is essential for the recognition of retinoic acid and various analogs.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- A mollusk retinoic acid receptor (RAR) ortholog sheds light on the evolution of ligand binding.Endocrinology · 2014Article
- Pharmacological activity of retinoic acid receptor alpha-selective antagonistsACS medicinal chemistry letters · 2013Article
- Oral administration of a retinoic Acid receptor antagonist reversibly inhibits spermatogenesis in mice.Endocrinology · 2011Article
- The eccentric cleavage product of β-carotene, β-apo-13-carotenone, functions as an antagonist of RXRα.Archives of biochemistry and biophysics · 2010Article
- Retinoid signaling during spermatogenesis as revealed by genetic and metabolic manipulations of retinoic acid receptor alpha.Society of Reproduction and Fertility supplement · 2007Review
- Review
- Analysis of the ligand-binding domain of human retinoic acid receptor alpha by site-directed mutagenesis.Molecular and cellular biology · 1996Article
- 4-Oxoretinol, a new natural ligand and transactivator of the retinoic acid receptors.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Utilizing a strategy involving domain exchange between retinoic acid receptors alpha and beta (RAR alpha and RAR beta) and monitoring the transcriptional activity of the resulting chimeric receptors with receptor-selective retinoids, we identified a 70-aa region within the N-terminal portion of the RAR alpha and -beta domain E which is important for an RAR alpha- or RAR beta-specific response. Two amino acid residues within this region, serine-232 (S232) and threonine-239 (T239) in RAR alpha and the corresponding alanine-225 (A225) and isoleucine-232 (I232) in RAR beta, were found to be essential for this effect. In addition, binding studies using the chimeric receptors expressed in Escherichia coli showed that the N-terminal portion of domain E was also important for the characteristic binding profile of t-RA and various retinoids with RAR alpha or RAR beta. Structural predictions of the primary amino acid sequence in this region indicate the presence of an amphipathic helix-turn-helix structure with five hydrophobic amino acids that resemble a leucine zipper motif. The amino acid residues identified by domain swapping, S232 and T239 in RAR alpha and A225 and I232 in RAR beta, were found within the hydrophobic face of an alpha-helix in close proximity to this zipper motif, suggesting that the ligand may interact with the receptor in the region adjacent to a surface involved in protein-protein interactions. This finding may link ligand binding to other processes important for transcriptional activation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.