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Molecular Dynamics Insights into TAS1R2 Transmembrane Domain Activation.

Yongcheng Lu1,2, Xinyi Ma1,2, Ziyue Meng1,2

  • 1Department of Pharmaceutical Sciences, School of Pharmacy and Pharmaceutical Sciences, BouvĂ© College of Health Sciences, Northeastern University, Boston, MA 02115, USA.

International Journal of Molecular Sciences
|December 11, 2025
PubMed
Summary
This summary is machine-generated.

Sweet taste receptors (STRs) function via TAS1R2/TAS1R3 heterodimers. Molecular dynamics simulations reveal distinct structural changes induced by agonists and antagonists, uncovering new insights into taste receptor activation mechanisms.

Keywords:
G-protein-coupled receptor (GPCR)MD simulationsconformational changesprotein-ligand interactionsreceptor activationsweet taste receptor

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Sweet taste receptors (STRs), class C G protein-coupled receptors (GPCRs), are TAS1R2/TAS1R3 heterodimers.
  • TAS1R2 alone or its transmembrane domain (TMD) can function as a receptor.
  • Previous studies indicated sweetener (S819) and inhibitor (amiloride) binding to TAS1R2-TMD, but mechanisms were unclear.

Purpose of the Study:

  • Investigate ligand-induced conformational dynamics of human TAS1R2-TMD (hTAS1R2-TMD).
  • Elucidate atomic-level mechanisms of STR activation by agonists and antagonists.
  • Provide a structural basis for designing novel sweeteners and taste modulators.

Main Methods:

  • Microsecond-scale molecular dynamics (MD) simulations.
  • Simulations performed on hTAS1R2-TMD bound to S819 (agonist), amiloride (antagonist), and in apo state.
  • Comparative analysis of conformational changes and interaction networks.

Main Results:

  • Agonist and antagonist binding distinctly modulate key structural switches, including the ionic lock (E6.35-R3.50).
  • A novel salt bridge (D7.32-R3.32) was identified, preferentially forming in the active state.
  • Ligand-specific rearrangements in hydrogen-bonding and hydrophobic networks were observed.

Conclusions:

  • Agonists and antagonists differentially modulate TAS1R2 activation through distinct structural mechanisms.
  • The novel D7.32-R3.32 salt bridge may act as a unique molecular switch for TAS1R2.
  • Findings offer atomistic insights and a structural foundation for designing new taste-modulating compounds.