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Title: Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1).
Authors: Tan, Joshua H.Y.
Ludeman, Justin P.
Wedderburn, Jamie
Canals, Meritxell
Hall, Pam
Butler, Stephen J.
Taleski, Deni
Christopoulos, Arthur
Hickey, Michael J.
Payne, Richard J.
Stone, Martin J.
Issue Date: 2013
Publisher: © American Society for Biochemistry and Molecular Biology
Citation: TAN, J.H.Y. ... et al, 2013. Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1). Journal of Biological Chemistry, 288 (14), pp. 10024 - 10034.
Abstract: 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.
Description: This article is closed access.
Sponsor: This work was supported by Australian Research Council Grants DP0881570 and LE0989504 (to M. J. S.) and DP1094884 (to R. J. P. and M. J. S.) and by Australian National Health and Medical Research Council Grant 519461 (to A. C.).
Version: Published
DOI: 10.1074/jbc.M112.447359
URI: https://dspace.lboro.ac.uk/2134/18766
Publisher Link: http://dx.doi.org/10.1074/jbc.M112.447359
ISSN: 0021-9258
Appears in Collections:Closed Access (Chemistry)

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