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• W2045120140 endingPage "623" @default.
• W2045120140 startingPage "611" @default.
• W2045120140 abstract "It became clear over the recent years that most, if not all, G protein-coupled receptors (GPCR) are able to form dimers or higher order oligomers. Chemokine receptors make no exception to this new rule and both homo- and heterodimerization were demonstrated for CC and CXC receptors. Functional analyses demonstrated negative binding cooperativity between the two subunits of a dimer. The consequence is that only one chemokine can bind with high affinity onto a receptor dimer. In the context of receptor activation, this implies that the motions of helical domains triggered by the binding of agonists induce correlated changes in the other protomer. The impact of the chemokine dimerization process in terms of co-receptor function and drug development is discussed." @default.
• W2045120140 created "2016-06-24" @default.
• W2045120140 creator A5051248437 @default.
• W2045120140 creator A5079381808 @default.
• W2045120140 creator A5088413885 @default.
• W2045120140 date "2005-12-01" @default.
• W2045120140 modified "2023-10-18" @default.
• W2045120140 title "Dimerization of chemokine receptors and its functional consequences" @default.
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