7t6v | pdb_00007t6v

Structure of the human FPR2-Gi complex with fMLFII

spinqualitylabelsall models 7t6v, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7t6v is a 6 chain structure with sequence from Bos taurus, Homo, Homo sapiens and Rattus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FME, PLM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FPR2_HUMAN Low affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophil chemotactic factors (PubMed:1374236). Binding of FMLP to the receptor causes activation of neutrophils (PubMed:1374236). This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system (PubMed:1374236). The activation of LXA4R could result in an anti-inflammatory outcome counteracting the actions of proinflammatory signals such as LTB4 (leukotriene B4) (PubMed:9547339). Receptor for the chemokine-like protein FAM19A5, mediating FAM19A5-stimulated macrophage chemotaxis and the inhibitory effect on TNFSF11/RANKL-induced osteoclast differentiation (By similarity).[UniProtKB:O88536] Publication Abstract from PubMed The formylpeptide receptors (FPRs) mediate pattern recognition of formylated peptides derived from invading pathogens or mitochondria from dead host cells. They can also sense other structurally distinct native peptides and even lipid mediators to either promote or resolve inflammation. Pharmacological targeting of FPRs represents a novel therapeutic approach in treating inflammatory diseases. However, the molecular mechanisms underlying FPR ligand recognition are elusive. We report cryo-EM structures of Gi-coupled FPR1 and FPR2 bound to a formylpeptide and Gi-coupled FPR2 bound to two synthetic peptide and small-molecule agonists. Together with mutagenesis data, our structures reveal the molecular mechanism of formylpeptide recognition by FPRs and structural variations of FPR1 and FPR2 leading to their different ligand preferences. Structural analysis also suggests that diverse FPR agonists sample a conserved activation chamber at the bottom of ligand-binding pockets to activate FPRs. Our results provide a basis for rational drug design on FPRs. Molecular recognition of formylpeptides and diverse agonists by the formylpeptide receptors FPR1 and FPR2.,Zhuang Y, Wang L, Guo J, Sun D, Wang Y, Liu W, Xu HE, Zhang C Nat Commun. 2022 Feb 25;13(1):1054. doi: 10.1038/s41467-022-28586-0. PMID:35217703 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transducin 3D structures

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