التفاصيل البيبلوغرافية
| العنوان: |
The human estrogen receptor α dimer binds a single SRC-1 coactivator molecule with an affinity dictated by agonist structure11Edited by K. Yamamoto |
| المؤلفون: |
Margeat, Emmanuel, Poujol, Nicolas, Boulahtouf, Abdelhay, Chen, Yan, Müller, Joachim D, Gratton, Enrico, Cavailles, Vincent, Royer, Catherine A |
| المصدر: |
Journal of Molecular Biology, vol 306, iss 3 |
| بيانات النشر: |
eScholarship, University of California |
| سنة النشر: |
2001 |
| المجموعة: |
University of California: eScholarship |
| مصطلحات موضوعية: |
Biochemistry and Cell Biology, Biological Sciences, Genetics, Estrogen, Underpinning research, 1.1 Normal biological development and functioning, Generic health relevance, Anisotropy, Base Sequence, Dimerization, Estrogen Receptor alpha, Histone Acetyltransferases, Humans, Ligands, Nuclear Receptor Coactivator 1, Protein Binding, Protein Structure, Quaternary, Receptors, Recombinant Fusion Proteins, Response Elements, Spectrometry, Fluorescence, Thermodynamics, Titrimetry, Transcription Factors, estrogen receptor, coactivator, affinity, photon counting histogram |
| جغرافية الموضوع: |
433 - 442 |
| الوصف: |
Nuclear receptors act as ligand-inducible transcription factors. Agonist binding leads to interaction with coactivator proteins, and to the assembly of the general transcription machinery. In addition to structural information, a thorough understanding of transcriptional activation by the nuclear receptors requires the characterization of the thermodynamic parameters governing these protein/protein interactions. In this study we have quantitatively characterized the interactions of full-length baculovirus expressed human estrogen receptor alpha (ERalpha), as well as ERalpha hormone binding domain (ERHBD) with a fragment of the coactivator protein SRC-1 (amino acid residues 570 to 780). Fluorescence anisotropy and fluorescence correlation spectroscopy of fluorescently labeled SRC-1(570-780) demonstrate unambiguously that the stoichiometry of the SRC-1/ERalpha/estradiol complex is one coactivator molecule per ERalpha dimer. The affinity of the estradiol or estriol bound ERalpha/SRC-1 complexes was found to be significantly higher than that observed in the presence of estrone. No binding was observed in the absence of ligand or in the presence of antagonists. Distinct anisotropy values for the ERalpha-SRC-1 complexes with different agonists suggest distinct conformations of the complexes depending upon agonist structure. |
| نوع الوثيقة: |
article in journal/newspaper |
| وصف الملف: |
application/pdf |
| اللغة: |
unknown |
| العلاقة: |
qt9p08t66m; https://escholarship.org/uc/item/9p08t66mTest |
| الإتاحة: |
https://escholarship.org/uc/item/9p08t66mTest |
| حقوق: |
CC-BY |
| رقم الانضمام: |
edsbas.BF93280D |
| قاعدة البيانات: |
BASE |
