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Related Concept Videos

Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
Intracellular Hormone Receptors01:08

Intracellular Hormone Receptors

Lipid-soluble hormones diffuse across the plasma and nuclear membrane of target cells to bind to their specific intracellular receptors. These receptors act as transcription factors that regulate gene expression and protein synthesis in the target cell
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...

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Updated: May 29, 2026

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
10:51

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists

Published on: November 15, 2013

Nuclear hormone receptor co-repressors: structure and function.

Peter J Watson1, Louise Fairall, John W R Schwabe

  • 1Henry Wellcome Laboratories of Structural Biology, Department of Biochemistry, University of Leicester, Leicester LE1 9HN, UK.

Molecular and Cellular Endocrinology
|September 20, 2011
PubMed
Summary
This summary is machine-generated.

Co-repressor proteins like SMRT and NCoR act as intrinsically disordered hubs, integrating transcription factors and histone modifiers. Recent structural studies reveal complex assembly mechanisms and interaction specificity, offering therapeutic targets.

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Biochemical Reconstitution of Steroid Receptor&#x2022;Hsp90 Protein Complexes and Reactivation of Ligand Binding
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Published on: September 21, 2011

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Last Updated: May 29, 2026

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
10:51

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists

Published on: November 15, 2013

Biochemical Reconstitution of Steroid Receptor&#x2022;Hsp90 Protein Complexes and Reactivation of Ligand Binding
11:07

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

Published on: September 21, 2011

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Epigenetics

Background:

  • Co-repressor proteins, including Silencing Mediator for Retinoid and Thyroid hormone receptors (SMRT) and Nuclear Receptor Coregulator (NCoR), are crucial for gene regulation.
  • These proteins function as "hub proteins," integrating transcription factor activity with histone modification enzymes.
  • Their intrinsically disordered nature presents significant challenges for structural determination.

Purpose of the Study:

  • To elucidate the structural basis of co-repressor protein interactions.
  • To understand the mechanism of co-repressor complex assembly.
  • To identify potential therapeutic targets within these interactions.

Main Methods:

  • X-ray crystallography and Nuclear Magnetic Resonance (NMR) spectroscopy were employed to determine the structures of co-repressor interaction regions.
  • Biochemical assays were used to analyze complex formation and specificity.

Main Results:

  • Several structures of co-repressor interaction domains bound to partners have been determined.
  • These structures provide insights into the assembly of large co-repressor complexes.
  • The structural data illuminate the basis for interaction specificity between co-repressors and their partners.

Conclusions:

  • Despite their disordered character, structural studies of co-repressor complexes are feasible and highly informative.
  • Understanding these protein-protein interactions is key to deciphering gene repression mechanisms.
  • The identified interaction interfaces represent promising targets for therapeutic intervention.