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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 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...
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,...

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Allostery and cooperativity revisited.

Qiang Cui1, Martin Karplus

  • 1Department of Chemistry and Theoretical Chemistry Institute, University of Wisconsin, Madison, Wisconsin 53706, USA.

Protein Science : a Publication of the Protein Society
|June 19, 2008
PubMed
Summary
This summary is machine-generated.

This review revisits allosteric regulation, showing that modern "population shift" models are rooted in older concepts. It integrates atomistic simulations to explain allosteric mechanisms beyond classical models.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Computational Biology

Background:

  • Allosteric regulation is crucial for biological processes.
  • Classical models (KNF, MWC) describe cooperativity but lack atomistic detail.
  • Recent studies aim to elucidate allosteric mechanisms at the atomic level.

Purpose of the Study:

  • To review the current understanding of allosteric mechanisms.
  • To compare new findings with classical models (MWC, KNF).
  • To highlight the historical context of the
  • population shift
  • view.

Main Methods:

  • Review of theoretical and computational studies.
  • Analysis of atomistic simulations of allosteric systems.
  • Comparison of simulation data with established allosteric models.

Main Results:

  • Allosteric mechanisms extend beyond classical MWC/KNF descriptions.
  • The
  • population shift
  • concept in allostery has historical precedence.
  • Atomistic simulations provide new insights into allosteric pathways.

Conclusions:

  • The
  • new view
  • of allostery is essentially an
  • old view
  • with modern computational support.
  • Understanding allostery requires integrating theoretical, computational, and experimental approaches.
  • This review resolves outstanding issues in allosteric regulation theory.