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