Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1). Joshua H.Y. Tan Justin P. Ludeman Jamie Wedderburn Meritxell Canals Pam Hall Stephen Butler Deni Taleski Arthur Christopoulos Michael J. Hickey Richard J. Payne Martin J. Stone 2134/18766 https://repository.lboro.ac.uk/articles/journal_contribution/Tyrosine_sulfation_of_chemokine_receptor_CCR2_enhances_interactions_with_both_monomeric_and_dimeric_forms_of_the_chemokine_monocyte_chemoattractant_protein-1_MCP-1_/9395834 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. 2015-09-15 13:59:47 untagged Chemical Sciences not elsewhere classified