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Related Concept Videos

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Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
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Full-length nuclear receptor allosteric regulation.

Woong Jae Choi1, Zeinab Haratipour2, Raymond D Blind3

  • 1Division of Diabetes, Endocrinology and Metabolism, Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA.

Journal of Lipid Research
|June 25, 2023
PubMed
Summary
This summary is machine-generated.

Nuclear receptors are regulated by lipids. This study explores how full-length nuclear receptor structures, including multidomain interactions, may be allosterically regulated by lipids.

Keywords:
Full-length nuclear receptorlipid regulation of full-length nuclear receptorlipid regulation of transcriptionlipid structural biologystructural interfaces

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Nuclear receptors are transcription factors regulated by diverse lipids.
  • They possess DNA-binding (DBD) and ligand-binding domains (LBDs).
  • Lipid binding to LBDs allosterically regulates receptor function and coregulator recruitment.

Purpose of the Study:

  • To investigate allosteric regulation of full-length nuclear receptors by lipids.
  • To evaluate interdomain interfaces as potential sites for lipid-mediated allosteric control.
  • To bridge the gap between isolated LBD studies and full-length receptor mechanisms.

Main Methods:

  • Analysis of published full-length nuclear receptor structures.
  • Examination of multidomain interactions within these receptors.
  • Evaluation of potential allosteric regulatory sites.

Main Results:

  • Few studies describe full-length nuclear receptor structures.
  • Even fewer describe lipid allosteric regulation of full-length receptors.
  • Interdomain interfaces are potential sites for lipid-induced allosteric regulation.

Conclusions:

  • Understanding full-length nuclear receptor structure-function relationships is crucial.
  • Lipids may allosterically regulate nuclear receptors via interdomain interfaces.
  • This research opens new avenues for drug development targeting nuclear receptor signaling.