CCR2 Antagonist

CCR2 Antagonist is a cell-permeable cis-diamidocyclohexyl urea compound with high affinity binding to CKR-2B (chemokine receptor 2; CCR2), also designated CD192. CKR-2B is a G protein-coupled receptor with a unique conserved glutamic acid residue in transmembrane 7, Glu291. Research shows that this conserved residue is a critical site for small molecule antagonist binding. MCP-1 (chemokine ligand 2; CCL2) is a specific chemokine for the CKR-2B receptor and is responsible for recruiting monocytes, memory T cells, and dendritic cells to sites of tissue injury and infection. CCR2 Antagonist displays high affinity binding for CKR-2B ( IC₅₀ = 5.1 nM) and potent functional antagonism (calcium flux IC₅₀ = 18 nM and chemotaxis IC₅₀ = 1 nM). Although Glu291 is a key receptor residue for CKR-2B, CCR2 Antagonist studies show that this inhibitor is not reliant upon Glu291 for its affinity binding, rather a nearby site. CCR2 Antagonist exhibits preferential binding for CKR-2B over CKR-3 (CCR3).