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Related Experiment Videos

The nicotinic acetylcholine receptor: a typical 'allosteric machine'.

Jean-Pierre Changeux1,2

  • 1CNRS UMR 3571, Institut Pasteur, Paris 75724, France changeux@noos.fr.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|May 9, 2018
PubMed
Summary

Allosteric interactions, distinct from competitive binding, involve protein conformational changes. Recent studies reveal the acetylcholine nicotinic receptor (nAChR) as an allosteric machine, guiding new drug development.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Allosteric interactions were first described for bacterial enzymes and later extended to membrane receptors.
  • These interactions involve distinct binding sites and reversible protein conformational changes, differing from classical competitive binding.
  • The acetylcholine nicotinic receptor (nAChR) exemplifies allosteric signaling, linking ligand binding to ion channel activity.

Purpose of the Study:

  • To elucidate the allosteric mechanisms governing signal transduction in receptors like the nAChR.
  • To investigate the structural basis of allosteric modulation and its role in receptor function.
  • To explore the potential for developing novel pharmacological agents based on allosteric modulation.

Main Methods:

Keywords:
allosteric modulationallosteric proteinmolecular machinenicotinic acetylcholine receptor

Related Experiment Videos

  • High-resolution X-ray crystallography and electron microscopy to determine nAChR structures.
  • Atomistic molecular dynamics simulations to model conformational transitions.
  • Analysis of allosteric modulator binding sites and their influence on receptor function.

    • Main Results:

    • Revealed a stepwise quaternary conformational transition in nAChR homologues.
    • Identified changes in subunit interfaces that host orthosteric and allosteric sites during the transition.
    • Demonstrated that nAChR functions as a typical allosteric machine.

    Conclusions:

    • The structural and dynamic insights into nAChR allostery provide a foundation for rational drug design.
    • Allosteric modulation of nAChR offers a promising strategy for developing new therapeutics.
    • Understanding allosteric machines like nAChR is crucial for advancing molecular pharmacology.