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Many different peptides with different frameworks and beginnings have now been characterized as FPR2 ligands. Nevertheless, the ligand-binding modes of FPR2 remain elusive, thus restricting the development of possible medications. Here we report the crystal structure of FPR2 bound into the potent peptide agonist WKYMVm at 2.8 Å quality. The dwelling adopts an active conformation and displays a deep ligand-binding pocket. Combined with mutagenesis, ligand binding and signaling researches,