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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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Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.
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Antigen binding allosterically promotes Fc receptor recognition.

Jun Zhao1, Ruth Nussinov2,3, Buyong Ma2

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|September 14, 2018
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Summary

Antigen binding to antibodies allosterically influences Fc receptor (FcR) binding. This communication, primarily via conformational population shifts, is crucial for FcR activation and therapeutic antibody design.

Keywords:
allosteric effectsallosteryantibodyconformational selection

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Area of Science:

  • Immunology
  • Structural Biology
  • Biophysics

Background:

  • Antibody function relies on Fab-antigen recognition and Fc receptor (FcR) interactions.
  • The role of antibody domains (Fab, Fc) and glycans in synergistic or independent modulation of activity remains unclear.
  • Understanding allosteric linkage between antigen binding and FcR engagement is critical for therapeutic antibody development.

Purpose of the Study:

  • To investigate the allosteric communication between antibody antigen recognition and Fc receptor binding.
  • To elucidate the conformational changes in antibody domains and glycans upon antigen and FcR binding.
  • To determine the mechanism by which antigen binding influences FcR interaction.

Main Methods:

  • Molecular dynamics simulations of four antibody complexes: free, antigen-bound, FcR-bound, and antigen-antibody-FcR.
  • Analysis of conformational populations and binding site accessibility.
  • Identification of allosteric communication pathways.

Main Results:

  • Antigen binding induces a conformational shift in the antibody, opening the Fc receptor binding site.
  • Fc-glycan-receptor complexes exhibit distinct conformational clusters related to antigen presence.
  • Allosteric communication occurs through IgG domains, but population shifts are the dominant mechanism.

Conclusions:

  • Antigen binding allosterically modulates Fc receptor recognition through conformational population shifts.
  • This antigen-driven communication mechanism is vital for FcR activation.
  • Findings provide insights into antibody allostery for improved therapeutic antibody design.