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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 communication between ACE2 active site and binding interface with SARS-CoV-2.

Mauro L Mugnai1, D Thirumalai1,2

  • 1Department of Chemistry, The University of Texas at Austin, Austin, Texas 78712, USA.

The Journal of Chemical Physics
|June 1, 2023
PubMed
Summary
This summary is machine-generated.

SARS-CoV-2 binding to ACE2 influences enzyme activity. Complex dissociation opens the ACE2 binding cleft, revealing a key glycine residue involved in disassembly.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Virology

Background:

  • Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) invades cells using its receptor binding domain (RBD) to bind Angiotensin-Converting Enzyme 2 (ACE2).
  • Understanding the dynamics of the RBD-ACE2 interaction is crucial for developing antiviral strategies.
  • Previous studies focused on binding affinity and mutation effects, but the allosteric consequences of dissociation were less explored.

Purpose of the Study:

  • To investigate the allosteric signal triggered by the dissociation of the SARS-CoV-2 RBD-ACE2 complex.
  • To elucidate the structural and dynamical changes in ACE2 upon complex disassembly.
  • To identify key residues involved in the dissociation process.

Main Methods:

  • Elastic Network Model (ENM) was constructed to represent the ACE2-RBD complex.
  • Structural Perturbation Method (SPM) was employed to analyze the effects of complex dissociation.
  • Computational modeling was used to study protein dynamics and allosteric signaling.

Main Results:

  • Complex dissociation leads to the opening of the ACE2 substrate-binding cleft, located distal to the RBD interface.
  • SARS-CoV-2 RBD binding facilitates fluctuations within the ACE2 binding cleft.
  • A conserved glycine residue (G502 in SARS-CoV-2) was identified as critical for complex disassembly.

Conclusions:

  • The study provides a structural and dynamical basis for how SARS-CoV-2 binding affects ACE2 enzymatic activity.
  • Dissociation of the RBD-ACE2 complex induces significant conformational changes in ACE2.
  • Targeting the identified key glycine residue could be a potential strategy for disrupting viral binding.