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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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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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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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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
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Protein Allostery at Atomic Resolution.

Dean Strotz1, Julien Orts1, Harindranath Kadavath1

  • 1Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, 8093, Zürich, Switzerland.

Angewandte Chemie (International Ed. in English)
|August 16, 2020
PubMed
Summary
This summary is machine-generated.

Protein allostery, the communication between distant protein sites, was studied using the Pin1 enzyme. Ligands were found to modulate protein dynamics, shifting its functional states and revealing mechanisms of dynamic allostery.

Keywords:
NMR spectroscopyallosteryligand bindingprotein dynamicsprotein structure

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Dynamics

Background:

  • Protein allostery involves long-range communication between distal sites in proteins.
  • Understanding allosteric mechanisms at atomic resolution is crucial for drug discovery.

Purpose of the Study:

  • To elucidate the allosteric mechanisms of the ligand-binding WW domain of the enzyme Pin1 at atomic resolution.
  • To investigate how different ligands modulate protein dynamics and function.

Main Methods:

  • Multistate structures were calculated using exact nuclear Overhauser effect (eNOE) data.
  • Analysis of protein conformational exchange and ligand-induced population shifts.

Main Results:

  • The free Pin1 WW domain exists in a microsecond exchange between two functional states.
  • A positive allosteric ligand shifts the equilibrium towards domain-domain interaction via a population shift model.
  • An allosteric-suppressing ligand disrupts inter-domain interactions by altering side-chain arrangements.

Conclusions:

  • The study reveals distinct modes of dynamic allostery in the Pin1 WW domain.
  • Protein dynamics play a critical role in mediating biological activity and allosteric regulation.
  • These findings offer insights into the design of allosteric modulators.