The N-formyl peptide receptor (FPR) family is comprised of three members, FPR, FPR3 (also designated FPRL1, lipoxin A4 receptor, FPRH1 or FPR2) and FPR like-2 (FPRL2), all of which are chemotactic G protein-coupled receptors that contain seven transmembrane domains. These receptors are found on the surface of phagocytic leukocytes, such as neutrophils and monocytes, and each family member contains specific residues, which are responsible for determining its ligand specificity. FPR3 is a promiscuous receptor that binds to several ligands, including lipoxin A4, N-formyl-methionyl-leucyl-phenylalanine (fMLP), serum amyloid A (SAA), prion peptide and the 42aa form of beta amyloid. Upon activation, FPR3 induces migration and calcium mobilization in human monocytes and neutrophils and is involved in inflammatory and host defense responses. FPR3 may mediate inflammation in prion and Alzheimer’s diseases, which makes it a potential target for therapeutic agents.