Cited by 107Estrogen and related hormone effectsReceptor Mechanisms and SignalingNuclear Receptors and Signaling

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Allosteric Control of Ligand Selectivity between Estrogen Receptors α and β

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Nettles, Kendall W., Sun, Jun, Radek, James T., Sheng, Shubin, Rodriguez, Alice L., Katzenellenbogen, John A., Katzenellenbogen, Benita S., Greene, Geoffrey L.·2004·Molecular Cell

DOI 10.1016/s1097-2765(04)00054-1

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Abstract

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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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: Nettles, Kendall W.
Sun, Jun
Sheng, Shubin
Rodriguez, Alice L.
Katzenellenbogen, John A.
Katzenellenbogen, Benita S.
Greene, Geoffrey L.
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2004-02
Volume: 13
Issue: 3
Pages: 317-327
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/s1097-2765(04)00054-1
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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Allosteric Control of Ligand Selectivity between Estrogen Receptors α and β

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