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Related Experiment Videos

Structural basis of RXR-DNA interactions.

Q Zhao1, S A Chasse, S Devarakonda

  • 1Department of Pharmacology X-ray Crystallography Laboratory, University of Virginia, Charlottesville, VA, 22908, USA.

Journal of Molecular Biology
|February 12, 2000
PubMed
Summary

The 9-cis retinoic acid receptor (RXR) structure reveals how DNA binding induces conformational changes for gene regulation. This explains how RXR homodimers bind DNA through specific protein-protein interactions and DNA target site spacing.

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Area of Science:

  • Molecular biology
  • Structural biology
  • Genetics

Background:

  • 9-cis retinoic acid receptor (RXR) is a nuclear receptor crucial for gene regulation.
  • RXR functions as a homodimer or heterodimer, binding to direct repeat DNA sequences with varying spacing.
  • Understanding RXR's DNA binding mechanism is key to deciphering gene transcription control.

Purpose of the Study:

  • To determine the crystal structure of the RXR DNA-binding domain as a homodimer bound to its DNA target.
  • To elucidate the molecular mechanisms of RXR-DNA interaction and conformational changes upon binding.
  • To understand how gene regulatory sites influence transcription factor assembly and function.

Main Methods:

  • X-ray crystallography at 2.1 Å resolution.

Related Experiment Videos

  • Co-crystallization of the RXR DNA-binding domain (DBD) with a direct repeat DNA target.
  • Structural analysis of the RXR homodimer-DNA complex.

    • Main Results:

    • The crystal structure reveals the RXR DBD homodimer bound to its direct repeat DNA target.
    • DNA binding induces conformational changes, including disruption of an alpha-helix in the T-box, facilitating dimerization and DNA binding.
    • RXR exhibits relaxed sequence recognition, interacting with three base pairs in each half-site.

    Conclusions:

    • The structure provides insights into homo-cooperative assembly driven by gene-regulatory sites.
    • RXR achieves DNA site selection through protein-protein interactions and specific DNA target site configurations.
    • This study clarifies the structural basis for RXR's role in eukaryotic transcription regulation.