Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1).

Background: Chemokine receptors are post-translationally sulfated on tyrosine residues. Results: A tyrosine-sulfated fragment of CCR2 binds more tightly to the monomeric form than the dimeric form of the chemokine MCP-1. Conclusion: Binding to sulfated CCR2 promotes conversion of MCP-1 from inactive dimer to active monomer. Significance: Tyrosine sulfation may regulate the ability of chemokine receptors to be activated by chemokines.