Chemokine receptors play fundamental roles in human physiology from embryogenesis to inflammatory response. The receptors belong to the G-protein coupled receptor class, and are activated by chemokine ligands with a range of specificities and affinities that result in a complicated network of interactions. The molecular basis for function is largely a black box, and can be directly attributed to the lack of structural information on the receptors. Studies to date indicate that function can be best described by a two-site model, that involves interactions between the receptor N-domain and ligand N-terminal loop residues (site-I), and between receptor extracellular loop and the ligand N-terminal residues (site-II). In this review, we describe how the two-site model could modulate binding affinity and ligand selectivity, and also highlight some of the unique chemokine receptor features, and their role in function.
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November 09 2006
Structural Basis of Chemokine Receptor Function—A Model for Binding Affinity and Ligand Selectivity
Lavanya Rajagopalan;
Lavanya Rajagopalan
1Department of Biochemistry and Molecular Biology and Sealy Center for Structural Biology, The University of Texas Medical Branch, Galveston, TX, 77555-1055, USA
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Krishna Rajarathnam
Krishna Rajarathnam
1Department of Biochemistry and Molecular Biology and Sealy Center for Structural Biology, The University of Texas Medical Branch, Galveston, TX, 77555-1055, USA
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Publisher: Portland Press Ltd
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 2006 Springer Science+Business Media, LLC
2006
Biosci Rep (2006) 26 (5): 325–339.
Citation
Lavanya Rajagopalan, Krishna Rajarathnam; Structural Basis of Chemokine Receptor Function—A Model for Binding Affinity and Ligand Selectivity. Biosci Rep 9 November 2006; 26 (5): 325–339. doi: https://doi.org/10.1007/s10540-006-9025-9
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