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Structural and Dynamics Insights into Melatonin Binding to MT1 Receptor.

Clementina Acconcia1, Antonella Paladino2, Francesca Scebba3

  • 1Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania "L. Vanvitelli", Caserta, Italy.

Chembiochem : a European Journal of Chemical Biology
|May 15, 2026
PubMed
Summary
This summary is machine-generated.

Melatonin (MLT) binding to the MT1 receptor was studied using nuclear magnetic resonance and computational methods. This research reveals how MLT interacts within the MT1 receptor's binding pocket under physiological conditions.

Keywords:
MT1‐receptormelatoninmolecular dynamics simulationon‐cell membrane NMR spectroscopy

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Pharmacology

Background:

  • Melatonin (MLT) regulates circadian rhythms via MT1 and MT2 receptors.
  • MLT exhibits diverse physiological effects, including antioxidant and neuroprotective properties.
  • High-resolution structural data on MLT binding to MT1 under physiological conditions is lacking.

Purpose of the Study:

  • To elucidate the high-resolution structural and dynamic details of melatonin (MLT) binding to the MT1 receptor.
  • To investigate MLT-MT1 interactions under near-native physiological conditions.

Main Methods:

  • High-resolution nuclear magnetic resonance (NMR) interaction studies on isolated cellular membranes overexpressing MT1 receptors.
  • Computational methodologies including homology modeling, molecular docking, and molecular dynamics simulations.

Main Results:

  • Melatonin (MLT) engages in hydrophobic interactions within the MT1 receptor's orthosteric binding pocket.
  • MLT binding enhances receptor motions, promoting local rearrangements in the MT1 receptor's cytoplasmic region.

Conclusions:

  • This study provides significant structural and dynamical insights into the MT1 receptor-melatonin (MLT) interaction.
  • The findings clarify the molecular mechanisms underlying MLT's action at the MT1 receptor level.