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Frances Sladek1

  • 1Department of Cell Biology and Neuroscience, University of California, Riverside 92521, USA.

Molecular Cell
|August 23, 2002
PubMed
Summary
This summary is machine-generated.

Researchers discovered fatty acids bound within the human hepatocyte nuclear factor 4 gamma (HNF4gamma) receptor. This finding challenges the understanding of nuclear receptors and suggests a novel evolutionary origin for these proteins.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Evolution

Background:

  • Hepatocyte nuclear factor 4 gamma (HNF4gamma) is a nuclear receptor.
  • Nuclear receptors are crucial transcriptional regulators.
  • HNF4gamma has been considered an "orphan" receptor due to an unidentified endogenous ligand.

Purpose of the Study:

  • To determine the high-resolution structure of the ligand binding domain of human HNF4gamma.
  • To identify potential endogenous ligands for HNF4gamma.
  • To understand the implications of ligand binding on receptor function and evolution.

Main Methods:

  • High-resolution X-ray crystallography was employed.
  • The structure of the ligand binding domain of human HNF4gamma was elucidated.

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Main Results:

  • Fatty acids were found to occupy the ligand binding pocket of HNF4gamma.
  • These fatty acids appear to be tightly bound and not easily exchanged.
  • The structure reveals a unique ligand-binding mode for this nuclear receptor.

Conclusions:

  • The discovery of bound fatty acids in HNF4gamma suggests a new paradigm for nuclear receptor function.
  • This finding provides insights into the evolutionary origins of nuclear receptors.
  • HNF4gamma may not function as a typical ligand-inducible receptor.