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Structural plasticity in the oestrogen receptor ligand-binding domain

Academic Article
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Overview

authors

  • Nettles, Kendall
  • Bruning, John
  • Gil, G.
  • O'Neill, E. E.
  • Nowak, J.
  • Guo, Y.
  • Kim, Y.
  • DeSombre, E. R.
  • Dilis, R.
  • Hanson, R. N.
  • Joachimiak, A.
  • Greene, G. L.

publication date

  • 2007

journal

  • EMBO Reports  Journal

abstract

  • The steroid hormone receptors are characterized by binding to relatively rigid, inflexible endogenous steroid ligands. Other members of the nuclear receptor superfamily bind to conformationally flexible lipids and show a corresponding degree of elasticity in the ligand-binding pocket. Here, we report the X-ray crystal structure of the oestrogen receptor alpha (ERalpha) bound to an oestradiol derivative with a prosthetic group, ortho- trifluoromethlyphenylvinyl, which binds in a novel extended pocket in the ligand-binding domain. Unlike ER antagonists with bulky side groups, this derivative is enclosed in the ligand-binding pocket, and acts as a potent agonist. This work shows that steroid hormone receptors can interact with a wider array of pharmacophores than previously thought through structural plasticity in the ligand-binding pocket.

subject areas

  • Cell Line, Tumor
  • Crystallography, X-Ray
  • Estradiol
  • Estrogen Receptor alpha
  • Humans
  • Ligands
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
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Identity

PubMed Central ID

  • PMC2002528

International Standard Serial Number (ISSN)

  • 1469-221X

Digital Object Identifier (DOI)

  • 10.1038/sj.embor.7400963

PubMed ID

  • 17468738
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Additional Document Info

start page

  • 563

end page

  • 568

volume

  • 8

issue

  • 6

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