Application of Circular Dichroism Spectroscopy to the Analysis of the Interaction Between the Estrogen Receptor Alpha and Coactivators: The Case of Calmodulin

  • Emeric Miclet
  • Sandrine Bourgoin-Voillard
  • Cillian Byrne
  • Yves Jacquot
Part of the Methods in Molecular Biology book series (MIMB, volume 1366)


The estrogen receptor α ligand-binding domain (ERα-LBD) binds the natural hormone 17β-estradiol (E2) to induce transcription and cell proliferation. This process occurs with the contribution of protein and peptide partners (also called coactivators) that can modulate the structure of ERα, and therefore its specificity of action. As with most transcription factors, ERα exhibits a high content of α helix, making it difficult to routinely run spectroscopic studies capable of deciphering the secondary structure of the different partners under binding conditions. Ca2+-calmodulin, a protein also highly structured in α-helix, is a key coactivator for ERα activity. Here, we show how circular dichroism can be used to study the interaction of ERα with Ca2+-calmodulin. Our approach allows the determination not only of the conformational changes induced upon complex formation but also the dissociation constant (Kd) of this interaction.

Key words

Estrogenreceptor Calmodulin Circular dichroism Peptide Helix content Kd 



We are grateful to the French Ministry of Research (ED387, iViv), the Centre National pour la Recherche Scientifique (CNRS) and the Université Pierre et Marie Curie (UPMC) for financial support.


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Copyright information

© Springer Science+Business Media New York 2016

Authors and Affiliations

  • Emeric Miclet
    • 1
  • Sandrine Bourgoin-Voillard
    • 2
    • 3
    • 4
    • 5
  • Cillian Byrne
    • 1
  • Yves Jacquot
    • 1
  1. 1.Laboratoire des Biomolécules, Sorbonne Universités, UPMC Univ Paris 06, CNRS-UMR 7203Université Pierre et Marie Curie-Ecole Normale SupérieureParis Cedex 05France
  2. 2.Plateforme Protéomique PROMETHEE, IAB, University Grenoble Alpes-INSERMInstitut de Biologie et de Pathologie,Grenoble, France; Equipe deSpectrométrie de masse, Institut Parisien de Chimie MoléculaireParisFrance
  3. 3.INSERM, IAB, Plateforme Protéomique PROMETHEEGrenobleFrance
  4. 4.CHU de Grenoble, IAB, Institut de Biologie et de Pathologie, Plateforme Protéomique PROMETHEEGrenobleFrance
  5. 5.Equipe de Spectrométrie de masse, Institut Parisien de Chimie Moléculaire, UMR 7201UPMC University Paris 06Paris Cedex 05France

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