The DOI matches its Crossref record, with a small difference in title or year; 40 of the 40 references it cites were found in a registry or an index.
Allosteric Control of Ligand Selectivity between Estrogen Receptors α and β
Open accessAbstract
Allosteric communication between interacting molecules is fundamental to signal transduction and many other cellular processes. To better understand the relationship between nuclear receptor (NR) ligand positioning and the formation of the coactivator binding pocket, we investigated the determinants of ligand selectivity between the two estrogen receptor subtypes ERalpha and ERbeta. Chimeric receptors and structurally guided amino acid substitutions were used to demonstrate that distinct "hot spot" amino acids are required for ligand selectivity. Residues within the ligand binding pocket as well as distal secondary structural interactions contribute to subtype-specific positioning of the ligand and transcriptional output. Examination of other NRs suggests a mechanism of communication between the ligand and coactivator binding pockets, accounting for partial agonist and dimer-specific activity. These results demonstrate the importance of long-range interactions in the transmission of information through the ligand binding domain as well as in determining the ligand selectivity of closely related NR receptor subtypes.
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“Comparison of classes of structures enabled identification of common features across many structures and space groups, and allowed statistical analysis and characterization of subtle features within the noise of a single structure, as we previously used for dissecting estrogen receptor signaling (Bruning et al., 2010; Nettles et al., 2004, 2008).”
From Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases (2012) · cites this paper as Nettles et al., 2004
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Self-citationLigand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ
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Structure and specificity of nuclear receptor–coactivator interactionsPreprint
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Self-citationUnique response pathways are established by allosteric interactions among nuclear hormone receptors
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Sensitization of diabetic and obese mice to insulin by retinoid X receptor agonists
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Crystal Structure of a Heterodimeric Complex of RAR and RXR Ligand-Binding Domains
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Rosenfeld, M. G., Lunyak, V. V., & Glass, C. K. (2006) · Genes & Development · doi:10.1101/gad.1424806 · Cited by 952
Mechanism of the nuclear receptor molecular switch
Nagy, L. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.04.006 · Cited by 406
Nuclear Receptor Structure: Implications for Function
Bain, D. L., Heneghan, A. F., Connaghan, K. D., & Miura, M. T. (2006) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.031905.160308 · Cited by 366
Estrogen receptor (ER)-β isoforms: A key to understanding ER-β signaling
Leung, Y., Mak, P., Hassan, S., & Ho, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605676103 · Cited by 357
Mechanisms of Mineralocorticoid Action
Fuller, P. J., & Young, M. J. (2005) · Hypertension · doi:10.1161/01.hyp.0000193502.77417.17 · Cited by 324
Metadata
- Authors
- Nettles, K. W., Sun, J., Radek, J. T., Sheng, S., Rodriguez, A. L., Katzenellenbogen, J. A., Katzenellenbogen, B. S., & Greene, G. L.
- Affiliations
- University of Chicago (US)
- University of Illinois Urbana-Champaign (US)
- Corresponding author
- Greene, Geoffrey L.
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 13
- Issue
- 3
- Pages
- 317-327
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2052459433
- Cited by
- 99
- References
- 40
- Citations by year
- 2025: 3 · 2023: 3 · 2021: 2 · 2020: 1 · 2019: 4 · 2018: 1 · 2015: 3 · 2014: 3 · 2013: 4 · 2012: 6
- FWCI
- 8.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3454 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R01CA089489, 5R01 CA 18119, R01 CA89489, P30 CA14599-29, CA25836, R01CA018119, P30CA014599)
- National Institute of Diabetes and Digestive and Kidney Diseases (R37DK015556, 5R37DK-15556)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- estrogen receptor alpha, estrogen receptor beta, ligand selectivity, allosteric communication, nuclear receptors, ligand-binding domain, chimeric receptors, amino acid substitutions, long-range interactions, partial agonism, transcriptional output
- MeSH terms
- Allosteric Regulation, Amino Acid Sequence, Amino Acids, Animals, Binding Sites, Cell Nucleus, Humans, Ligands, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Protein Binding, Receptors, Estrogen, Recombinant Fusion Proteins, Protein Structure, Tertiary, Receptors, Cytoplasmic and Nuclear, COS Cells, Cell Line, Tumor, Estrogen Receptor alpha, Estrogen Receptor beta
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