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Related Concept Videos

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...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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 pathway,...
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...

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Related Experiment Video

Updated: May 19, 2026

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
11:19

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

A push-and-pull model for allosteric anion binding in cage complexes.

Johannes M Dieterich1, Guido H Clever, Ricardo A Mata

  • 1Institut für Physikalische Chemie, Universität Göttingen, Tammannstr. 6, 37077 Göttingen, Germany.

Physical Chemistry Chemical Physics : PCCP
|August 23, 2012
PubMed
Summary
This summary is machine-generated.

This study explains the allosteric effect in anion binding within a self-assembled Pd(II) cage. Ligand length and binding pocket flatness are key factors influencing this behavior.

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Area of Science:

  • Supramolecular Chemistry
  • Computational Chemistry
  • Coordination Chemistry

Background:

  • Anion binding hosts are crucial for molecular recognition and sensing.
  • Self-assembly offers a powerful route to complex supramolecular architectures.
  • Understanding allosteric effects is vital for designing sophisticated molecular systems.

Purpose of the Study:

  • To investigate the electronic structure of an artificial anion binding host.
  • To elucidate the mechanism behind the observed allosteric effect in anion binding.
  • To correlate computational findings with experimental observations.

Main Methods:

  • Electronic structure calculations were performed on a self-assembled Pd(II) cage.
  • A push-and-pull model was employed to analyze site potentials.
  • Ligand length and binding pocket characteristics were evaluated.

Main Results:

  • The self-assembly of four Pd(II) cations and eight pyridyl ligands forms an interpenetrated double cage with three binding pockets.
  • A push-and-pull model successfully explains the allosteric anion binding.
  • Potential flatness and ligand length were identified as critical factors for allosteric modulation.

Conclusions:

  • Computational results align well with experimental structures.
  • The study provides a mechanistic understanding of allosteric anion binding in a supramolecular host.
  • This work advances the design principles for functional anion receptors.