The human formylpeptide receptor subfamily of GPCRs (FPR: nomenclature described in [48,70] [1, 2]) comprises three members (FPR1, FPR2, and FPR3). Two of these, FPR1 and FPR2, recognize peptides bearing N-terminal formyl-Met from invading bacteria [29] or mitochondria. These peptides function as danger signals in innate immunity. FPR1 and FPR2 are promiscuous and also recognize several non-formylated peptides, proteins, lipids and small molecules [29,48,70] of which some are able to initiate signals (balanced or biased) that mediate pro-inflammatory and/or inflammation resolving effects [37,46]. In contrast, FPR3 remains less well-characterized in part due to the absence of selective ligands which has significantly impeded progress in its functional characterization [9,50].

Note that the data for FPR2 are also reproduced on the leukotriene receptor page under the heading "the FPR2/ALX receptor". It should also be noted that some of the specialized pro-resolving mediators are, in addition to the FPRs, also recognized by other GPCRs and they are present at very low levels as endogenous mediators for resolution of inflammation [52]. Since potency for different FPR agonists determined in many different research laboratories is dependent on the assay systems used, direct comparison of potency may be difficult for FPR agonists with anti-inflammatory and pro-resolving activities. For this reason, the pro-resolving lipid mediators are listed in one group and ligands with balanced agonistic activities are listed in another group for potency comparison. The biased signaling characteristics of some of the FPR agonists must be taken into consideration when their potencies are compared [21,35,60].
FPR1 has been reported to be the plague receptor on host immune cells [42] and as co-receptor for HIV [66], but these findings have to be further explored [20]. Some FPR2 ligands suggested to allosterically modulate receptor function activate the receptor in a classical but functionally selective mode [68], whereas allosteric modulatory effects of other compounds cause changes in receptor conformational states and receptor signaling [21]. The 3-D structure of FPR1/2 has been solved and the FPR2 structure reveals a large binding pocket that can accommodate ligands of different shapes and sizes for the generation of different conformational changes [33]. Studies have been conducted to explore the mechanisms by which primarily FPR2 mediates both pro-inflammatory and anti-inflammatory signaling in a ligand-dependent manner. It should be noted, however, that some of the not yet clearly identified anti-inflammatory signals, are generated by agonists that preferentially activate FPR1 [47]. The status of FPR2 dimerization is a determining factor for ligand-specific conformational changes leading to biased signaling [5]. There is also a report on ligand concentration-dependent dual modulation of FPR2 for receptor-activation vs. anti-inflammatory activities [19] , and ligand concentration-dependent modulation of FPR1 functions has also been reported [65]. FPR ligands are attractive candidates for promoting the resolution of inflammation, enhancing innate immune defense and tuning immune responses in inflammatory/auto-immune diseases and tumor microenvironments [6,64].

* Key recommended reading is highlighted with an asterisk

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* Dorward DA, Lucas CD, Chapman GB, Haslett C, Dhaliwal K, Rossi AG. (2015) The Role of Formylated Peptides and Formyl Peptide Receptor 1 in Governing Neutrophil Function during Acute Inflammation. Am J Pathol, 185 (5): 1172-1184. [PMID:25791526]

Gavins FN. (2010) Are formyl peptide receptors novel targets for therapeutic intervention in ischaemia-reperfusion injury?. Trends Pharmacol Sci, 31 (6): 266-76. [PMID:20483490]

* Krepel SA, Wang JM. (2019) Chemotactic Ligands that Activate G-Protein-Coupled Formylpeptide Receptors. Int J Mol Sci, 20 (14). [PMID:31336833]

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* Nunes VS, Abrahão Jr O, Rogério AP, Serhan CN. (2023) ALX/FPR2 Activation by Stereoisomers of D1 Resolvins Elucidating with Molecular Dynamics Simulation. J Phys Chem B, 127 (29): 6479-6486. [PMID:37428488]

* Nunes VS, Serhan CN, Abrahão Jr O, Rogério AP. (2025) ALX/FPR2 Receptor Activation by Inflammatory (fMLFII) and Pro-resolving (LXA₄ and RvD3) Agonists. ACS Phys Chem Au, 5 (4): 367-374. [PMID:40727226]

* Perretti M, Godson C. (2020) Formyl peptide receptor type 2 agonists to kick-start resolution pharmacology. Br J Pharmacol, 177 (20): 4595-4600. [PMID:32954491]

* Yazid S, Norling LV, Flower RJ. (2012) Anti-inflammatory drugs, eicosanoids and the annexin A1/FPR2 anti-inflammatory system. Prostaglandins Other Lipid Mediat, 98 (3-4): 94-100. [PMID:22123264]

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Subcommittee members: Richard D. Ye (Chairperson) School of Life and Health Sciences The Chinese University of Hong Kong, Shenzhen Guangdong, 518172 China François Boulay Commissariat à l’Energie Atomique Institut de Recherches en Technologies et Sciences pour le Vivant Laboratoire de Biochimie et de Biophysique des Systèmses Intégrés Grenoble France Claes Dahlgren Department of Rheumatology and Inflammation Research University of Göteborg Göteborg Sweden Craig Gerard Department of Pediatrics Harvard Medical School and Children's Hospital Boston Massachusetts U.S.A Philip M. Murphy Head, Molecular Signaling Section, Laboratory of Molecular Immunology, and Chief, Laboratory of Molecular Immunology National Institute of Allergy and Infectious Diseases National Institutes of Health 9000 Rockville Pike MSC-1888 Bldg. 10, Room 11N113 Bethesda MD 20892 USA Marc Parmentier Institut de Recherche Interdisciplinaire en Biologie Humaine et Moléculaire (IRIBHM) Université Libre de Bruxelles Brussels Belgium Mark Quinn Department of Microbiology and Immunology Montana State University Bozeman, MT 59717 U.S.A. Charles N. Serhan Center for Experimental Theraputics and Reperfusion Injury Brigham and Women's Hospital Hale Building for Transformative Medicine 60 Fenwood Road, Suite 3-016 Boston, MA 02115 USA

Other contributors: Magnus Bäck (Past contributor) Translational Cardiology Karolinska Institutet, Department of Medicine Karolinska University Hospital M85 141 86 Stockholm Sweden Nan Chiang (Past contributor) Center for Experimental Theraputics and Reperfusion Injury Brigham and Women's Hospital Hale Building for Transformative Medicine 60 Fenwood Road, Suite 3-016 Boston, MA 02115 USA Sven-Erik Dahlén (Past contributor) Unit for Experimental Asthma and Allergy Research The National Institute of Environmental Medicine Karolinska Institutet S-171 77 Stockholm Sweden Jeffrey Drazen (Past contributor) Respiratory Division Brigham and Woman's Hospital 75 Francis Street Boston, MA 02115 USA Jilly F. Evans (Past contributor) PharmAkea 12780 El Camino Real San Diego, CA 92130 USA Huamei Fu Forsman University of Göteborg Göteborg Sweden Helena Chengxue Qin Drug Discovery Biology Victorian Heart Institute Monash University Melbourne Australia G. Enrico Rovati (Past contributor) (Past contributor (deceased)) Formerly of the Laboratory of Molecular Pharmacology University of Milan Italy Takao Shimizu (Past contributor) National Center for Global Health and Medicine Shinjyuku Tokyo 166-8655 Japan Ji Ming Wang (Past contributor) Laboratory of Molecular Immunoregulation Cancer and Inflammation Program Center for Cancer Research National Cancer Institute at Frederick Frederick Maryland USA Takehiko Yokomizo (Past contributor) Department of Biochemistry Juntendo University School of Medicine Hongo 2-1-1 Bunkyo-ku Tokyo 113-8421 Japan