FPR1 Membrane Protein Introduction

Introduction of FPR1

FPR1, also referred to formyl peptide receptor 1, fMet-Leu-Phe receptor (fMLP receptor), N-formyl peptide receptor or N-formylpeptide chemoattractant receptor, is a 38.4 kDa cell surface receptor protein that belongs to the family of G protein-coupled pattern recognition receptors. In humans, this gene is located at the chromosome 19q13.41 and encodes a 350 amino acids protein. FPR1 is predominantly expressed on mammalian phagocytic leukocytes and is a key player in the host defense and innate immunity. This protein is a high-affinity receptor for fMLP, a powerful neutrophil chemotactic factor. Binding of fMLP to FPR1 receptor can stimulate intracellular calcium mobilization, together with superoxide anion release. This process is mediated by a G-protein which activates the phosphatidylinositol-calcium second messenger system.

Basic Information of FPR1
Protein Name fMet-Leu-Phe receptor
Gene Name FPR1
Aliases Formyl Peptide Receptor 1, FPR, FMLP, FMLP Receptor, N-Formyl Peptide Receptor, N-Formylpeptide Chemoattractant Receptor, FMet-Leu-Phe Receptor
Organism Homo sapiens (Human)
UniProt ID P21462
Transmembrane Times 7
Length (aa) 350

Function of FPR1 Membrane Protein

FPR1 is an essential chemotaxis receptor that involved in multiple aspects of host defense and inflammatory processes. It is found to be prominently expressed by mammalian phagocytic leukocytes where this receptor mediates cells' responses to the N-formylmethionine-containing oligopeptides. In neutrophils, signaling through FPR1 plays a role in chemotaxis, killing microorganisms through phagocytosis, and generating reactive oxygen species (ROS). Furthermore, it is considered to function in sensing endogenous signals of dysfunctional cells, which should guide leukocytes to the site of inflammation and tissue damage. A large number of ligands have been identified to trigger FPR1 including formylated and non-formylated peptides in endogenous and microbial origin. The first validated ligand for FPR1 is N-formylated peptides from bacteria, but later, it is found such N-formylated peptides also can derive endogenously from mitochondria, and are released as a result of severe cell dysfunction and cell death.

The structure of homology model of FPR1 and its binding pocket. Fig.1 The structure of homology model of FPR1 and its binding pocket. (Yuan, 2012)

Application of FPR1 Membrane Protein in Literature

  1. Jesaitis A. J., et al. Formyl Met-Leu-Phe-stimulated FPR1 phosphorylation in plate-adherent human neutrophils: enhanced proteolysis but lack of Inhibition by platelet-activating factor. J Immunol Res. 2018, 2018: 3178970. PubMed ID: 29785402

    N-formyl-Met-Leu-Phe (fMLF) is a model that PAMP/DAMP drives human PMN to sites of injury/infection by the GPCR and FPR1. The author speculated, although the conditions of the assay might trigger PAF-stimulated necrosis, the cell densities on the plates possibly approach levels found in inflamed tissues and provide for an explanation of PAF divergent influences on the FPR1 phosphorylation and PMN function.

  2. Morris S., et al. Whole blood FPR1 mRNA expression predicts both non-small cell and small cell lung cancer. Int J Cancer. 2018, 142(11): 2355-2362. PubMed ID: 29313979

    In whole blood, FPR1 mRNA levels can be used to predict the presence of lung cancer. Taking this as a reflex test for lung cancer screening computed tomography (CT) scans has the potential to elevate the positive predictive value. This marker is easily measured and monitored in an automated process via off-the-shelf equipment and reagents.

  3. Kirpotina L. N., et al. 4-Aroyl-3-hydroxy-5-phenyl-1H-pyrrol-2(5H)-ones as N-formyl peptide receptor 1 (FPR1) antagonists. Biochem Pharmacol. 2017, 142: 120-132. PubMed ID: 28690139

    Formyl peptide receptors (FPRs) are expressed in various leukocytes and play vital roles in inflammations. Therefore, 4-aroyl-3-hydroxy-5-phenyl-1H-pyrrol-2(5H)-one scaffold, represents a strong backbone for the development of novel FPR antagonists and can offer significant clues to understand the molecular structure of these antagonists.

  4. Yang S. C., et al. Dipeptide HCH6-1 inhibits neutrophil activation and protects against acute lung injury by blocking FPR1. Free Radic Biol Med. 2017, 1106: 254-269. PubMed ID: 28232203

    Formyl peptide receptor 1 (FPR1) is regarded as a new therapeutic target for the discovery of drugs to treat neutrophilic inflammations. The findings in this article suggested that a FPR1 antagonist, HCH6-1 (N-(N-benzoyl-L-tryptophanyl)-D-phenylalanine methyl ester), is likely to have great promising to be an emerging agent for treating FPR1-associated inflammatory lung diseases.

  5. Honda M., et al. Intravital Imaging of Neutrophil Recruitment Reveals the Efficacy of FPR1 Blockade in Hepatic Ischemia-Reperfusion InjuryJ Immunol. 2017, 198(4): 1718-1728. PubMed ID: 28062700

    This study is aimed to investigate the dynamic neutrophil recruitment by two-photon laser scanning microscopy (TPLSM) in response to FPR1 block in hepatic I/R. Authors’ finding suggested effective methods for clarifying the mechanisms of immune cell responses during hepatic I/R.

FPR1 Preparation Options

To obtain the native, stable and functional target membrane proteins, Creative Biolabs presents efficient reconstitution forms together with numerous active formats for these membrane proteins. Our versatile Magic™ membrane protein production platform provides many flexible choices, from which you can frequently find a better option for your specialized projects. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-FPR1 antibody development services.

All along Creative Biolabs has perfectly generated diverse functional membrane proteins to satisfy the needs of our customers. We are pleased to tailor one-stop, custom-oriented service packages in regard to varieties of membrane protein targets to be studied. Please feel free to contact us for more information.


  1. Yuan S, et al. (2012). The role of water in activation mechanism of human N-formyl peptide receptor 1 (FPR1) based on molecular dynamics simulations. PLoS One. 7(11), e47114.

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