Historical Background
Formyl peptide receptor 1 (FPR1) was first discovered on human neutrophils through its ability to bind N-formylated peptides with high affinity (Schiffmann et al. 1975). Rabbit neutrophils exhibit similar binding properties. The 350-amino acid human FPR1 receptor was the first cloned leukocyte chemoattractant receptor (Boulay et al. 1990). Genes with homologous sequence (FPR2 and FPR3) were identified through low-stringency hybridization using the FPR1 cDNA. The FPR2 cDNA encodes a 351-residue protein and shares approximately 69% sequence identity with FPR1. FPR2 is a low-affinity receptor for the prototypic formyl peptide, N-formyl-Met-Leu-Phe (fMLF). It binds lipoxin A4 and therefore is termed FPR2/ALX (Ye et al. 2009). FPR3 encodes a 7TM receptor of 352 amino acids that shares 56% sequence identity with FPR1 but does not bind fMLF. Although these three human members of the formyl peptide receptor family are relatively similar in terms...
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Southgate, E.L., Ye, R.D. (2018). Formyl Peptide Receptor. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_403
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DOI: https://doi.org/10.1007/978-3-319-67199-4_403
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