ArticleMolecular and cellular biology1999
Molecular determinants of the estrogen receptor-coactivator interface.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- In Silico Characterization of PathogenicGenes · 2025Article
- Characterization of novel small molecule inhibitors of estrogen receptor-activation function 2 (ER-AF2).Breast cancer research : BCR · 2024Article
- TRIM33 Is a Co-Regulator of Estrogen Receptor Alpha.Cancers · 2024Article
- ESR1 activating mutations: From structure to clinical application.Biochimica et biophysica acta. Reviews on cancer · 2023Review
- 17β-Estradiol Concentration and Direct βAnnals of neurosciences · 2022Article
- Review
- Application of the human estrogen receptor within a synthetic transcription factor inFungal biology and biotechnology · 2020Article
- Transactivation Function-1-Mediated Partial Agonist Activity of Selective Estrogen Receptor Modulator Requires Homo-Dimerization of the Estrogen Receptor α Ligand Binding Domain.International journal of molecular sciences · 2019Review
- Fibronectin rescues estrogen receptor α from lysosomal degradation in breast cancer cells.The Journal of cell biology · 2018Article
- Molecular mechanism of estrogen-estrogen receptor signaling.Reproductive medicine and biology · 2017Review
- Estradiol-Estrogen Receptor α Mediates the Expression of the CXXC5 Gene through the Estrogen Response Element-Dependent Signaling Pathway.Scientific reports · 2016Article
- Transactivation Function-2 of Estrogen Receptor α Contains Transactivation Function-1-regulating Element.The Journal of biological chemistry · 2015Article
- Aromatase-null mice expressing enhanced green fluorescent protein in germ cells provide a model system to assess estrogen-dependent ovulatory responses.Transgenic research · 2014Article
- Understanding nuclear receptor form and function using structural biology.Journal of molecular endocrinology · 2013Review
- Crystal structure of Fushi tarazu factor 1 ligand binding domain/Fushi tarazu peptide complex identifies new class of nuclear receptors.The Journal of biological chemistry · 2011Article
- Multiple-targeting and conformational selection in the estrogen receptor: computation and experiment.Chemical biology & drug design · 2011Article
- Minireview: Not picking pockets: nuclear receptor alternate-site modulators (NRAMs).Molecular endocrinology (Baltimore, Md.) · 2010Review
- Estrogen and progesterone receptors: from molecular structures to clinical targets.Cellular and molecular life sciences : CMLS · 2009Review
- The role of androgen receptor mutations in prostate cancer progression.Current genomics · 2009Article
- P160/SRC/NCoA coactivators form complexes via specific interaction of their PAS-B domain with the CID/AD1 domain.Nucleic acids research · 2008Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcriptional activation by the estrogen receptor is mediated through its interaction with coactivator proteins upon ligand binding. By systematic mutagenesis, we have identified a group of conserved hydrophobic residues in the ligand binding domain that are required for binding the p160 family of coactivators. Together with helix 12 and lysine 366 at the C-terminal end of helix 3, they form a hydrophobic groove that accommodates an LXXLL motif, which is essential for mediating coactivator binding to the receptor. Furthermore, we demonstrated that the high-affinity binding of motif 2, conserved in the p160 family, is due to the presence of three basic residues N terminal to the core LXXLL motif. The recruitment of p160 coactivators to the estrogen receptor is therefore likely to depend not only on the LXXLL motif making hydrophobic interactions with the docking surface on the receptor, but also on adjacent basic residues, which may be involved in the recognition of charged residues on the receptor to allow the initial docking of the motif.
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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.