Structural Determinants for the Interaction of Formyl Peptide Receptor 2 with Peptide Ligands * *This work was supported, in whole or in part, by National Basic Research Program of China (973 Program Grant 2012CB518000) and National Natural Science Foundation of China (Grant 31270941). This work was also supported by National Institutes of Health Grants R01 AI033503 and P01 HL077806, and by Specialized Research Fund for the Doctoral Program of Higher Education of China (Grant 20120073110069), the Ministerio de Ciencia e Innovacion (SAF2010-22198-C02-02) and the Instituto de Salud Carlos III (RD07/0067/0008) of Spain. This article contains supplemental Figs. 1 and 2.
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 289, Issue: 4, Page: 2295-2306
2014
- 57Citations
- 75Captures
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Metrics Details
- Citations57
- Citation Indexes57
- CrossRef57
- 55
- Captures75
- Readers75
- 75
Article Description
Unlike formyl peptide receptor 1 (FPR1), FPR2/ALX (FPR2) interacts with peptides of diverse sequences but has low affinity for the Escherichia coli- derived chemotactic peptide fMet-Leu-Phe (fMLF). Using computer modeling and site-directed mutagenesis, we investigated the structural requirements for FPR2 to interact with formyl peptides of different length and composition. In calcium flux assay, the N -formyl group of these peptides is necessary for activation of both FPR2 and FPR1, whereas the composition of the C-terminal amino acids appears more important for FPR2 than FPR1. FPR2 interacts better with pentapeptides (fMLFII, fMLFIK) than tetrapeptides (fMLFK, fMLFW) and tripeptide (fMLF) but only weakly with peptides carrying negative charges at the C terminus ( e.g. fMLFE). In contrast, FPR1 is less sensitive to negative charges at the C terminus. A CXCR4-based homology model of FPR1 and FPR2 suggested that Asp-281 7.32 is crucial for the interaction of FPR2 with certain formyl peptides as its negative charge may be repulsive with the terminal COO- group of fMLF and negatively charged Glu in fMLFE. Asp-281 7.32 might also form a stable interaction with the positively charged Lys in fMLFK. Site-directed mutagenesis was performed to remove the negative charge at position 281 in FPR2. The D281 7.32 G mutant showed improved affinity for fMLFE and fMLF and reduced affinity for fMLFK compared with wild type FPR2. These results indicate that different structural determinants are used by FPR1 and FPR2 to interact with formyl peptides.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820335833; http://dx.doi.org/10.1074/jbc.m113.509216; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84893106152&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/24285541; http://www.jbc.org/lookup/doi/10.1074/jbc.M113.509216; https://syndication.highwire.org/content/doi/10.1074/jbc.M113.509216; https://linkinghub.elsevier.com/retrieve/pii/S0021925820335833; https://dx.doi.org/10.1074/jbc.m113.509216; http://www.jbc.org/content/289/4/2295; http://www.jbc.org/article/S0021925820335833/abstract; http://www.jbc.org/article/S0021925820335833/fulltext; http://www.jbc.org/article/S0021925820335833/pdf; https://www.jbc.org/article/S0021-9258(20)33583-3/abstract; https://www.jbc.org/content/289/4/2295; http://www.jbc.org/cgi/doi/10.1074/jbc.M113.509216; http://www.jbc.org/content/289/4/2295.abstract; http://www.jbc.org/content/289/4/2295.full; http://www.jbc.org/content/289/4/2295.full.pdf; http://europepmc.org/abstract/med/24285541; http://europepmc.org/articles/PMC3900973
American Society for Biochemistry & Molecular Biology (ASBMB)
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