Special Issue "Chemokines"

Guest Editor
Dr. Mark Murphy
Research Immunology, Actelion Pharmaceuticals Ltd, Gewerbestrasse 16, CH- 4123 Allschwil, Switzerland
Website: http://www.actelion.com/
E-Mail: mark.murphy@actelion.com
Phone: +41 61 565 85 12
Interests: immunology; targeted therapies for inflammatory and autoimmune diseases; signal transduction pathways as innovative therapeutic targets; stem cells; protein-protein interactions; targeted therapies for cancer; cytokines/chemokines

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Type of Paper: Review
Title: Orthosteric and Allosteric Ligand Interactions within the Chemokine System-­‐Implications for Future Drug Design
Authors: Stefanie Thiele and Mette M. Rosenkilde
Affiliation: The Laboratory of Molecular Pharmacology, Department of Neuroscience and Pharmacology, University of Copenhagen, The Panum Institute, Copenhagen, DK-2200, Denmark
Abstract: Chemokine receptors are class A 7TM receptors, thereby belonging to the largest protein group in the human genome. Together with their peptide ligands they control cell migration, and have been targets for drug development resulting in numerous small molecule drug candidates. Given the large size and extracellular receptor interaction of chemokines with their receptors, small molecules often act in an allosteric mode with a site within the transmembrane domain, and studies showing their probe-­‐dependent and receptor-­‐dependent character are accumulating. This mode of action is in clear contrast to prototype class A 7TM receptors, such as the adrenergic receptors, or class C 7TM receptors in which small molecule allosteric sites are often found in the extracellular domains. Here, the structural knowledge on chemokine and small-­‐molecule ligand interaction with chemokine receptors is reviewed, providing the basis for understanding the diversity of allosteric interactions in chemokine receptors.