Multiple Binding Sites for Small Molecule Antagonists at the Chemokine Receptor CCR2

A.J. Zweemer, I. Nederpelt, H. Vrieling, S. Hafith, M.L. Doornbos, H. de Vries, J. Abt, R. Gross, D. Stamos, J. Saunders, M.J. Smit, A.P. IJzerman, L.H. Heitman

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The chemokine receptor CCR2 is a G protein-coupled receptor that is activated primarily by the endogenous CC chemokine ligand 2 (CCL2). Many different small-molecule antagonists have been developed to inhibit this receptor, as it is involved in a variety of diseases characterized by chronic inflammation. Unfortunately, all these antagonists lack clinical efficacy, and therefore a better understanding of their mechanism of action is warranted. In this study, we examined the pharmacological properties of small-molecule CCR2 antagonists in radioligand binding and functional assays. Six structurally different antagonists were selected for this study, all of which displaced the endogenous agonist
Original languageEnglish
Pages (from-to)551-561
JournalMolecular Pharmacology
Volume2013
Issue number84
DOIs
Publication statusPublished - 2013

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