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Related Concept Videos

Drug-Receptor Interaction: Agonist01:25

Drug-Receptor Interaction: Agonist

Agonists are drugs that interact with specific receptors in the body to produce a biological response. When an agonist binds to a receptor, it activates or enhances the receptor's function, leading to physiological effects. The interaction between agonist drugs and receptors is crucial for their therapeutic action in various medical treatments.
Agonists can bind to receptors in different ways. Some agonists bind directly to the receptor's active site, mimicking the endogenous ligand's action.
The Two-State Receptor Model01:29

The Two-State Receptor Model

The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with one...
Spare Receptors01:30

Spare Receptors

Some receptors remain unoccupied even when an agonist produces a maximal response. Such empty ones are called spare receptors. In presence of spare receptors the maximum effect of an agonist drug is achieved with fewer than 100% of the receptors being occupied. To determine the presence of spare receptors, scientists often compare the concentration of the drug needed to produce 50% of the maximum effect (EC50) with the concentration of the drug needed to occupy 50% of the receptors (Kd). If the...
Drug-Receptor Interactions01:29

Drug-Receptor Interactions

Drug-receptor interaction describes the binding of receptors by drugs, but not all drug-receptor interactions result in activation and tissue response. For instance, the binding of agonists activates the receptor to generate a cellular reaction, while antagonists bind to receptors without causing their activation.
Several parameters, such as the drug's affinity for its receptor and its efficacy, which is its ability to activate the receptor, determine the drug's effect on the tissue.
Opioid Receptors: Overview01:22

Opioid Receptors: Overview

Opioid receptors, including the mu (μ, MOR), delta (δ, DOR), and kappa (κ, KOR) types, belong to the rhodopsin family of G protein-coupled receptors. These receptors are located throughout the central and peripheral nervous systems and in non-neuronal tissues such as macrophages and astrocytes. Opioid receptor ligands can be categorized into agonists or antagonists. Highly selective agonists include [d-Ala2, MePhe4, Gly(ol)5]-enkephalin or DAMGO for MOR, [D-Pen2, D-Pen5]-enkephalin or DPDPE for...
Adrenergic Agonists: Chemistry and Structure-Activity Relationship01:16

Adrenergic Agonists: Chemistry and Structure-Activity Relationship

Adrenergic agonists' structure-activity relationship (SAR) determines their selectivity and efficacy. These agonists comprise a phenylethylamine moiety with an aromatic ring and an ethylamine side chain.
Aromatic ring substitutions: Substituting the aromatic ring with –OH groups at positions 3 and 4 yields catecholamines (e.g., epinephrine), which have a high affinity for adrenoceptors. Hydrogen bonding between –OH groups and receptors enhances adrenergic activity.
Separation of the aromatic...

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Quantifying Agonist Activity at G Protein-coupled Receptors
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Quantifying Agonist Activity at G Protein-coupled Receptors

Published on: December 26, 2011

Extending the IP3 receptor model to include competition with partial agonists.

Gregory A Handy1, Bradford E Peercy

  • 11000 Hilltop Circle, Department of Mathematics and Statistics, University of Maryland Baltimore County, Baltimore, MD 21250, USA. handy1@umbc.edu

Journal of Theoretical Biology
|June 21, 2012
PubMed
Summary

This study models how partial agonists affect inositol 1,4,5-trisphosphate receptors, revealing they can functionally mimic IP(3) knockdown and alter calcium signaling dynamics.

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A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

Area of Science:

  • Cellular Biology
  • Biophysics
  • Computational Biology

Background:

  • The inositol 1,4,5-trisphosphate (IP(3)) receptor is a critical Ca(2+) channel in the endoplasmic reticulum, regulating calcium signaling across diverse cell types.
  • Previous models by De Young and Keizer (1992) and Li and Rinzel (1994) described IP(3) receptor dynamics.
  • Recent work by Rossi et al. (2009) investigated the impact of partial agonists (PA) on IP(3) receptor function.

Purpose of the Study:

  • To extend the existing IP(3) receptor model to incorporate the competitive binding of partial agonists.
  • To analyze the structure-function relationship between IP(3) and its receptor in the presence of PAs.
  • To investigate the effects of PAs on whole-cell calcium dynamics, including wave propagation.

Main Methods:

  • Extended the eight-state IP(3) receptor model to a 12-state model to account for partial agonist competition.
  • Performed a model reduction to a two-variable system, similar to Li and Rinzel (1994).
  • Integrated the reduced model into a two-dimensional cell model to simulate calcium wave propagation.

Main Results:

  • The extended model successfully illustrates the competitive binding between IP(3) and partial agonists for the receptor.
  • Optimizing subunit affinities for IP(3) and PAs provided a good fit to experimental data from Rossi et al. (2009).
  • Partial agonists were found to induce qualitatively different calcium dynamics compared to simple IP(3) reduction.

Conclusions:

  • Partial agonists can functionally act as IP(3) knockdown, altering calcium signaling pathways.
  • The developed model provides a framework for understanding partial agonist effects on IP(3) receptor-mediated calcium release.
  • This research offers insights into the complex regulation of cellular calcium signaling by modulators of the IP(3) receptor.