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ALX/FPR2 Receptor Activation by Inflammatory (fMLFII) and Pro-resolving (LXA4 and RvD3) Agonists.

Vinicius S Nunes1, Charles N Serhan2, Odonírio Abrahão3

  • 1Programa de Pós-Graduação em Produtos Bioativos e Biociências, Universidade Federal do Rio de Janeiro, Avenida Aluizio da Silva Gomes 50, Macaé 27930-560, Brasil.

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Summary

Investigating the ALX/FPR2 receptor activation, this study found that residues R201 and R205 are key for both pro-resolution and pro-inflammatory agonists, with D106 only interacting with fMLFII.

Keywords:
ALX/FPR2 receptorGPCRinflammationlipoxin A4molecular dynamicspro-resolving mediatorsresolvin RvD3

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • The ALX/FPR2 receptor plays a role in inflammatory and resolution pathways.
  • Previous structural data suggests D106, R201, and R205 are involved in receptor activation.

Purpose of the Study:

  • To investigate ALX/FPR2 receptor activation mechanisms using computational simulations.
  • To compare the effects of pro-resolution agonists (LXA4, RvD3) and a pro-inflammatory agonist (fMLFII).

Main Methods:

  • Docking simulations and long-term molecular dynamics simulations were employed.
  • Analysis included receptor activation state, electrostatic interactions, and binding affinities (MM/PBSA).

Main Results:

  • LXA4 and fMLFII maintained receptor activation longer than RvD3.
  • Residues R201 and R205 were critical for all tested agonists.
  • fMLFII, but not LXA4 or RvD3, interacted with residue D106.
  • Electrostatic interactions significantly contributed to agonist-receptor binding.

Conclusions:

  • R201 and R205 are essential for ALX/FPR2 activation by diverse agonists.
  • D106's role in activation appears specific to certain agonists like fMLFII.
  • This study enhances understanding of ALX/FPR2 activation by pro-resolution and inflammatory molecules.