The N-formyl peptide receptor (FPR) family is comprised of three members, FPR, FPR2 (also designated lipoxin A4 receptor, FPRH1 and FPRL1) and FPR3 (also designated 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. FPR2 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 42 amino acid form of ∫ amyloid. Upon activation, FPR2 induces migration and calcium mobilization in human monocytes and neutrophils and is involved in inflammatory and host defense responses. FPR2 may mediate inflammation in prion and Alzheimer’s diseases, which makes it a potential target for therapeutic agents.