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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Synthesis and Regulation of Thyroid Hormones01:20

Synthesis and Regulation of Thyroid Hormones

Low blood levels of the thyroid hormones — triiodothyronine (T3) and thyroxine (T4) — signal the hypothalamus to release the thyrotropin-releasing hormone (TRH). TRH then reaches the pituitary gland and stimulates the release of thyroid-stimulating hormone(TSH) into the bloodstream.
Upon reaching the thyroid gland, TSH stimulates the follicular cells' active uptake of iodide ions from the blood. The ions diffuse to the apical surface of the cells and are oxidized to iodine. The iodine is then...

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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

The allosteric modulation of thyroxine-binding globulin affinity is entropy driven.

Ariel A Petruk1, María S Labanda, Rosa M S Alvarez

  • 1Instituto Superior de Investigaciones Biológicas, Tucumán, Argentina. apetruk@fbqf.unt.edu.ar

Biochimica Et Biophysica Acta
|March 6, 2013
PubMed
Summary

Thyroxine-binding globulin (TBG) allosteric regulation is driven by conformational entropy changes. Multiple stressed states (S states) of TBG may enhance thyroxine (T4) release, aiding protease activity.

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Last Updated: May 13, 2026

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • Thyroxine-binding globulin (TBG) is a serpin protein crucial for thyroxine (T4) transport.
  • TBG undergoes a stressed-to-relaxed (S-to-R) transition upon reactive center loop (RCL) cleavage, which reduces T4 affinity.
  • Previous studies showed no significant structural differences in the T4 binding site across different TBG states.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying T4 affinity regulation by TBG based on the degree of RCL insertion.
  • To investigate the thermodynamic basis of T4 binding to TBG in various conformational states.

Main Methods:

  • Extended molecular dynamics simulations were employed.
  • Thermodynamic analysis of T4 binding to TBG was performed.
  • Simulations covered three distinct S states and the R state of TBG.

Main Results:

  • T4 binding interactions were similar across all TBG states.
  • A strong correlation was observed between the extent of RCL insertion and T4 binding affinity.
  • The observed affinity changes were primarily driven by alterations in TBG's conformational entropy.

Conclusions:

  • TBG's allosteric regulation of T4 affinity is fundamentally entropy-driven.
  • The existence of multiple S states potentially facilitates more efficient T4 release.
  • Computational simulations provide insights into the thermodynamic basis of allosteric regulation in serpins.