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Allosteric Regulation01:08

Allosteric Regulation

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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...
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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...
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Allosteric Proteins-ATCase01:19

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Quantifying Agonist Activity at G Protein-coupled Receptors
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The Quantitative Characterization of Functional Allosteric Effects.

Terry Kenakin1

  • 1Department of Pharmacology, University of North Carolina School of Medicine, Chapel Hill, North Carolina.

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PubMed
Summary
This summary is machine-generated.

This study details molecular parameters for measuring positive allosteric modulators (PAMs) and negative allosteric modulators (NAMs) that interact with G protein-coupled receptors (GPCRs). Understanding these interactions is key for developing new allosteric drugs targeting GPCRs.

Keywords:
allostericallosteric drugsdrug activityquantifying drug activity

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Molecular Biology

Background:

  • Seven-transmembrane receptors (7TMRs), also known as G protein-coupled receptors (GPCRs), are crucial for cell signaling.
  • Allosteric drugs, including positive allosteric modulators (PAMs) and negative allosteric modulators (NAMs), represent a significant class of therapeutics targeting GPCRs.

Purpose of the Study:

  • To describe the molecular parameters used to quantify the interactions of PAMs and NAMs with GPCRs.
  • To provide a framework for understanding allosteric modulation of GPCR function.

Main Methods:

  • Review of molecular parameters relevant to allosteric modulation.
  • Analysis of ligand-receptor interactions at distinct binding sites.

Main Results:

  • Identification and definition of key molecular parameters for measuring allosteric modulator efficacy.
  • Quantification of PAM and NAM interactions with GPCRs.

Conclusions:

  • Accurate measurement of molecular parameters is essential for characterizing PAM and NAM activity.
  • This work facilitates the rational design and development of allosteric drugs targeting GPCRs.