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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.
Butler, Stephen J.
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
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
|Publisher Link: ||http://dx.doi.org/10.1074/jbc.M112.447359|
|Appears in Collections:||Closed Access (Chemistry)|
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