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Related Experiment Videos

Structural elements of an orphan nuclear receptor-DNA complex

Q Zhao1, S Khorasanizadeh, Y Miyoshi

  • 1Department of Pharmacology, School of Medicine, University of Virginia, Charlottesville 22908, USA.

Molecular Cell
|July 14, 1998
PubMed
Summary
This summary is machine-generated.

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Nuclear hormone receptors use a second DNA-binding interface for specificity. This finding expands our understanding of how these transcription factors recognize diverse DNA response elements.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Nuclear hormone receptors are the largest transcription factor family.
  • Current models of DNA discrimination by these receptors are insufficient to explain specificity among over 150 nonsteroid receptors.
  • Existing models focus on a single hexameric half-site and a conserved DNA-binding domain (DBD).

Purpose of the Study:

  • To elucidate the structural basis of DNA recognition by the orphan receptor RevErb.
  • To investigate how nuclear hormone receptors achieve specificity in binding to DNA response elements.
  • To understand the role of tandem homodimerization in receptor-DNA interaction.

Main Methods:

  • X-ray crystallography to determine the 2.3 A crystal structure of the RevErb DNA-binding region.

Related Experiment Videos

  • Analysis of the protein-DNA complex formed by RevErb on its optimal response element.
  • Sequence comparison of orphan receptors to identify conserved and unique features.

    • Main Results:

    • The crystal structure revealed a tandem homodimer arrangement of the RevErb DNA-binding region on DNA.
    • A second, previously undescribed protein-DNA interface was identified adjacent to the classical half-site interaction.
    • Sequence analysis suggests unique minor-groove interactions involving receptor hinge regions contribute to DNA and dimerization specificity.

    Conclusions:

    • The DNA-binding mechanism of nuclear hormone receptors is more complex than previously thought.
    • RevErb utilizes a tandem homodimerization mode with an additional protein-DNA interface for specific binding.
    • Hinge region interactions are critical for conferring DNA and dimerization specificity in orphan receptors, expanding the understanding of transcription factor-DNA recognition.