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DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex

Academic Article
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Overview

authors

  • Zhang, J.
  • Chalmers, Michael
  • Stayrook, K. R.
  • Burris, L. L.
  • Wang, Y. J.
  • Busby, S. A.
  • Pascal, B. D.
  • Garcia-Ordonez, R. D.
  • Bruning, John
  • Istrate, M. A.
  • Kojetin, Douglas
  • Dodge, J. A.
  • Burris, Thomas
  • Griffin, Patrick

publication date

  • March 2011

journal

  • Nature Structural & Molecular Biology  Journal

abstract

  • The vitamin D receptor (VDR) functions as an obligate heterodimer in complex with the retinoid X receptor (RXR). These nuclear receptors are multidomain proteins, and it is unclear how various domains interact with one another within the nuclear receptor heterodimer. Here, we show that binding of intact heterodimer to DNA alters the receptor dynamics in regions remote from the DNA-binding domains (DBDs), including the coactivator binding surfaces of both co-receptors, and that the sequence of the DNA response element can determine these dynamics. Furthermore, agonist binding to the heterodimer results in changes in the stability of the VDR DBD, indicating that the ligand itself may play a role in DNA recognition. These data suggest a mechanism by which nuclear receptors show promoter specificity and have differential effects on various target genes, providing insight into the function of selective nuclear receptor modulators.

subject areas

  • Binding Sites
  • Dihydroxycholecalciferols
  • Humans
  • Ligands
  • Models, Molecular
  • Nuclear Receptor Coactivator 1
  • Promoter Regions, Genetic
  • Protein Interaction Domains and Motifs
  • Protein Interaction Mapping
  • Protein Stability
  • Protein Structure, Tertiary
  • Receptors, Calcitriol
  • Retinoid X Receptors
  • Tretinoin
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Identity

PubMed Central ID

  • PMC3087838

International Standard Serial Number (ISSN)

  • 1545-9985

Digital Object Identifier (DOI)

  • 10.1038/nsmb.2046

PubMed ID

  • 21478866
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Additional Document Info

start page

  • 556

end page

  • 563

volume

  • 18

issue

  • 5

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